Biomolecular NMR Assignments最新文献

¹H, ¹³C and ¹⁵N chemical shift assignment for stem-loop 5a from the 5'UTR of HCoV-229E. 从HCoV-229E的5'UTR中，茎环5a的1H， 13C和15N化学位移分配。

IF 0.6 4区生物学

Biomolecular NMR Assignments Pub Date : 2025-07-31 DOI: 10.1007/s12104-025-10243-4

Nina M Krause, Anna Wacker, Christian Richter, Boris Fürtig, Ramakanth Madhugiri, John Ziebuhr, Harald Schwalbe

引用次数: 0

Backbone NMR assignments of the essential oxidoreductase tryparedoxin from the human pathogenic parasite Trypanosoma cruzi. 人类致病性克氏锥虫必需氧化还原酶tryparedoxin的核磁共振骨架分配。

IF 0.6 4区生物学

Biomolecular NMR Assignments Pub Date : 2025-07-28 DOI: 10.1007/s12104-025-10244-3

Eric Schwegler, Ute A Hellmich

{"title":"Backbone NMR assignments of the essential oxidoreductase tryparedoxin from the human pathogenic parasite Trypanosoma cruzi.","authors":"Eric Schwegler, Ute A Hellmich","doi":"10.1007/s12104-025-10244-3","DOIUrl":"https://doi.org/10.1007/s12104-025-10244-3","url":null,"abstract":"Over 7 million people worldwide are affected with Chagas disease, a lifelong debilitating and potentially fatal Neglected Tropical Disease caused by the single cell protozoan parasite Trypanosoma cruzi. To maintain viability and to reproduce under the harsh conditions within a host organism, pathogens express a variety of protecting enzymes and virulence factors that can serve as potential drug targets. To protect itself from redox stress, T. cruzi takes advantage of a unique thiol metabolism. For instance, a cytosolic peroxide clearance cascade is centered on the conserved oxidoreductase Tryparedoxin (Tpx). Tpx efficiently distributes reducing equivalents across the parasitic cell through the promiscuous yet selective binding of numerous up- and downstream clients. However, the exact structure and binding interfaces of this central protein binding hub remain unknown. To study the redox-dependent structural dynamics of T. cruzi Tpx, and its interactions with binding partners, we determined the 1H, 13C, 15N-backbone NMR assignments of the enzyme in the reduced and oxidized state. In agreement with earlier NMR studies on Tpx from related protozoans, we report redox-dependent changes in the enzyme's dithiol active site that could play a crucial role in the recognition of physiological substrates and should be considered in the rational design of small molecule inhibitors.","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":" ","pages":""},"PeriodicalIF":0.6,"publicationDate":"2025-07-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144726342","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

¹H, ¹³C, ¹⁵N backbone chemical shift assignment of P18ink4c from Danio rerio (zebrafish) using solution-state NMR spectroscopy. 利用溶液态核磁共振光谱分析斑马鱼P18ink4c的1H， 13C， 15N主链化学位移。

IF 0.6 4区生物学

Biomolecular NMR Assignments Pub Date : 2025-07-28 DOI: 10.1007/s12104-025-10245-2

Aakriti Sethi, Pierre de Cordovez, Biswaranjan Mohanty, Vanessa K Morris, Christoph Göbl

引用次数: 0

Backbone assignment of a 28.5 kDa class A extended spectrum β-lactamase by high-field, carbon-detected solid-state NMR. 一个28.5 kDa的a类扩展光谱β-内酰胺酶的高场碳检测固体核磁共振骨架分配。

IF 0.6 4区生物学

Biomolecular NMR Assignments Pub Date : 2025-07-27 DOI: 10.1007/s12104-025-10242-5

Christopher G Williams, Songlin Wang, Alexander F Thome, Owen A Warmuth, Varun Sakhrani, Leighton Coates, Chad M Rienstra, Leonard J Mueller

引用次数: 0

NMR chemical shift assignment of UEV domain of ubiquitin-conjugating enzyme E2 variant 3 lactate dehydrogenase (UEVLD). 泛素偶联酶E2变体3乳酸脱氢酶（UEVLD） UEV结构域的NMR化学位移赋值。

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2025-06-26 DOI: 10.1007/s12104-025-10240-7

Jose G Vazquez, David A Nyenhuis, Marie-Paule Strub, Nico Tjandra

{"title":"NMR chemical shift assignment of UEV domain of ubiquitin-conjugating enzyme E2 variant 3 lactate dehydrogenase (UEVLD).","authors":"Jose G Vazquez, David A Nyenhuis, Marie-Paule Strub, Nico Tjandra","doi":"10.1007/s12104-025-10240-7","DOIUrl":"https://doi.org/10.1007/s12104-025-10240-7","url":null,"abstract":"UEV domains are catalytically dead variants of the E2 enzymes which play an intermediate role in ubiquitin signaling. UEV domain containing proteins, like the ESCRT-I factor Tsg101 often play critical roles in trafficking of ubiquitylated cargos or in modulating ubiquitin processivity, or in determining the type of signal that is transferred to a target protein. Ubiquitin-conjugating enzyme E2 variant (UEV) and lactate/malate dehydrogenase (UEVLD), also known as UEV3, is a human paralogue of Tsg101 with apparent associations to cancer, innate immunity, NF-κB signaling, and autophagy. It contains an N-terminal UEV domain with 56% identity to that of Tsg101 and a C-terminal lactate dehydrogenase domain. Here, we show the backbone assignments of the UEV domain from UEVLD and find that its Cα shifts are consistent with a UEV domain composition. Further experiments suggest that it may have regions corresponding to the known binding pockets of Tsg101, but further structural and functional work will be required to uncover critical determinants of UEV domain function, and the role of these domains in Ubiquitin signaling as a whole.","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":" ","pages":""},"PeriodicalIF":0.8,"publicationDate":"2025-06-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144504408","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Resonance assignment of the intrinsically disordered actin-binding region of Drebrin. 德雷布林内在无序动作蛋白结合区的共振分配。

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2025-06-14 DOI: 10.1007/s12104-025-10239-0

Soma Varga, Julie Maibøll Kaasen, Zoltán Gáspári, Bálint Ferenc Péterfia, Frans A A Mulder

{"title":"Resonance assignment of the intrinsically disordered actin-binding region of Drebrin.","authors":"Soma Varga, Julie Maibøll Kaasen, Zoltán Gáspári, Bálint Ferenc Péterfia, Frans A A Mulder","doi":"10.1007/s12104-025-10239-0","DOIUrl":"https://doi.org/10.1007/s12104-025-10239-0","url":null,"abstract":"Drebrin (developmentally regulated brain protein) is a vital component of the Postsynaptic Density (PSD). It performs important biological roles as it interacts with the postsynaptic protein Homer and anchors the complete protein network to the cellular skeleton through actin filaments. Drebrin contains unique structural elements including an evolutionarily unconventional actin-depolymerizing factor homology (ADFH) domain that has lost its strong actin-binding ability, and a Single Alpha-Helix (SAH) motif harbored by long flexible regions. In vivo studies have suggested that a disordered segment in Drebrin plays a key role in binding filamentous actin, yet the atomic-level characterization of the binding interface between these proteins has not been reported. To bridge this gap, we designed the intrinsically disordered construct D233 and employed 3D (HN)CO(CO)NH NMR spectroscopy to accomplish a near-complete backbone resonance assignment. This work serves as an essential step toward a detailed structural and functional investigation of the interaction between Drebrin and F-Actin.","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":" ","pages":""},"PeriodicalIF":0.8,"publicationDate":"2025-06-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144293164","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

¹H, ¹⁵N and ¹³C backbone resonance assignment of the N-terminal region of Zika virus NS4B protein in detergent micelles. 寨卡病毒 NS4B 蛋白 N 端区域在洗涤剂胶束中的 1H、15N 和 13C 骨架共振分配。

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2025-06-01 Epub Date: 2024-11-07 DOI: 10.1007/s12104-024-10208-z

Yan Li, Ying Ru Loh, Qingxin Li, Dahai Luo, CongBao Kang

引用次数: 0

Chemical shift assignments of N-terminal dsRNA binding domains dsRBD1 and dsRBD2 of Arabidopsis thaliana DRB5. 拟南芥DRB5 n端dsRNA结合域dsRBD1和dsRBD2的化学位移定位

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2025-06-01 Epub Date: 2025-03-24 DOI: 10.1007/s12104-025-10224-7

Priti Chanda Behera, Sneha Paturi, Mandar V Deshmukh

引用次数: 0

¹H, ¹⁵N, ¹³C backbone resonance assignment of human Alkbh7. 人Alkbh7的1H， 15N， 13C骨干共振分配。

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2025-06-01 Epub Date: 2025-01-29 DOI: 10.1007/s12104-025-10219-4

Baboucarr Faal, Jeffrey A Purslow, Vincenzo Venditti

{"title":"1H, 15N, 13C backbone resonance assignment of human Alkbh7.","authors":"Baboucarr Faal, Jeffrey A Purslow, Vincenzo Venditti","doi":"10.1007/s12104-025-10219-4","DOIUrl":"10.1007/s12104-025-10219-4","url":null,"abstract":"The Alkbh7 protein, a member of the Alkylation B (AlkB) family of dioxygenases, plays a crucial role in epigenetic regulation of cellular metabolism. This paper focuses on the NMR backbone resonance assignment of Alkbh7, a fundamental step in understanding its three-dimensional structure and dynamic behavior at the atomic level. Herein, we report the backbone 1H, 15N, 13C chemical shift assignment of the full-length human Alkbh7. Experiments were acquired at 25 °C by heteronuclear multidimensional NMR spectroscopy. Collectively, 70% of the backbone NH resonances were assigned, with 144 out of a possible 205 residues assigned in the 1H-15N TROSY spectrum. Interestingly, peaks from the active site and the C-terminal end of Alkbh7 are not NMR visible, suggesting that these regions are dynamic on the intermediate exchange regime. Using the program TALOS+, a secondary structure prediction was generated from the assigned backbone resonance that is consistent with the previously reported X-ray structure of the enzyme. The reported assignment will permit investigations of the protein structural dynamics anticipated to provide crucial insight regarding fundamental aspects in the recognition and enzyme regulation processes.","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":" ","pages":"65-69"},"PeriodicalIF":0.8,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12116241/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143062988","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Backbone resonance assignments of dopamine N-acetyltransferase in free and cofactor-bound states. 游离和辅因子结合状态下多巴胺n -乙酰转移酶的主链共振分配。

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2025-06-01 Epub Date: 2025-02-12 DOI: 10.1007/s12104-025-10222-9

Chu-Ya Wu, Yi-Zong Lee, I-Chen Hu, Liang-Yuan Chiu, Wei-Cheng Ding, Jing Wang, Shih-Che Sue, Shin-Ichi Tate, Ping-Chiang Lyu

{"title":"Backbone resonance assignments of dopamine N-acetyltransferase in free and cofactor-bound states.","authors":"Chu-Ya Wu, Yi-Zong Lee, I-Chen Hu, Liang-Yuan Chiu, Wei-Cheng Ding, Jing Wang, Shih-Che Sue, Shin-Ichi Tate, Ping-Chiang Lyu","doi":"10.1007/s12104-025-10222-9","DOIUrl":"10.1007/s12104-025-10222-9","url":null,"abstract":"Dopamine N-acetyltransferase (Dat), belonging to the GCN5-related N-acetyltransferase (GNAT) superfamily, is an arylalkylamine N-acetyltransferase (AANAT) that is involved in insects neurotransmitter inactivation and the development of insect cuticle sclerotization. By using the cofactor acetyl coenzyme A (Ac-CoA) as an acetyl group donor, Dat produces acetyl-dopamine through the reaction with dopamine. Although AANATs share similar structural features with the GNAT family, they have low sequence identities among insect AANATs (~ 40%) and between insect AANATs and vertebrate AANATs (~ 12%). A common noticed feature in GNATs is the Ac-CoA-binding induced conformational change, and this is important for further selection and catalysis of its substrate. In AANATs, the conformational changes help the sequential binding mechanism. Here, we report the 1H, 13C and 15N backbone resonance assignments of the 24 kDa Dat from Drosophila melanogaster in the free and Ac-CoA-bound states, and the chemical shift differences revealed a significant conformational change in the α1 region of Dat. These assignments provide a foundation for further investigations of the catalysis and structural regulation of Dat in solution.","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":" ","pages":"83-93"},"PeriodicalIF":0.8,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12116598/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143397713","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0