Biomolecular NMR Assignments最新文献

Backbone resonance assignments of dopamine N-acetyltransferase in free and cofactor-bound states.

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub 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":"https://doi.org/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":""},"PeriodicalIF":0.8,"publicationDate":"2025-02-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","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":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Backbone resonance assignment of the catalytic and ATP-binding domain of CpxA from Escherichia coli.

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2025-02-07 DOI: 10.1007/s12104-025-10218-5

Jing Deng, Guofang Zeng, Wenqing Xia, Wei Tang, Zhaofei Chai, Yixiang Liu, Conggang Li, Liqun Huang, Ling Jiang

引用次数: 0

¹H, ¹³C, ¹⁵N and ³¹P chemical shift assignment of the first stem-loop Guanidine-II riboswitch from Escherichia coli.

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2025-02-01 DOI: 10.1007/s12104-025-10217-6

Tatjana Koob, Silas Döpp, Harald Schwalbe

引用次数: 0

¹H, ¹⁵N, ¹³C backbone resonance assignment of human Alkbh7.

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub 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":""},"PeriodicalIF":0.8,"publicationDate":"2025-01-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","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":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Chemical shift assignments of DRB2 domains, a dsRNA binding protein in A. thaliana RNAi pathway.

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2025-01-29 DOI: 10.1007/s12104-025-10220-x

Upasana Rai, Debadutta Patra, Mandar V Deshmukh

引用次数: 0

Backbone assignment of the N-terminal domain of the A subunit of the Bacillus cereus GerI germinant receptor. 蜡样芽孢杆菌GerI生发受体A亚基n端结构域的骨架分配。

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2025-01-18 DOI: 10.1007/s12104-025-10216-7

Yulia Pustovalova, Yunfeng Li, Jeffrey C Hoch, Bing Hao

引用次数: 0

Assignment of the N-terminal domain of mouse cGAS. 小鼠cGAS n端结构域的定位。

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2025-01-04 DOI: 10.1007/s12104-024-10213-2

Hanna Aucharova, Rasmus Linser

引用次数: 0

Backbone NMR resonance assignment of Sis1, a type B J-domain protein from Saccharomyces cerevisiae. 酿酒酵母菌B型j结构域蛋白Sis1的核磁共振骨架结构。

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2024-12-30 DOI: 10.1007/s12104-024-10212-3

Glaucia M S Pinheiro, Gisele C Amorim, Carolina O Matos, Carlos H I Ramos, Fabio C L Almeida

{"title":"Backbone NMR resonance assignment of Sis1, a type B J-domain protein from Saccharomyces cerevisiae.","authors":"Glaucia M S Pinheiro, Gisele C Amorim, Carolina O Matos, Carlos H I Ramos, Fabio C L Almeida","doi":"10.1007/s12104-024-10212-3","DOIUrl":"https://doi.org/10.1007/s12104-024-10212-3","url":null,"abstract":"J-domain proteins (JDPs) are essential cochaperones of heat shock protein 70 (Hsp70), as they bind and deliver misfolded polypeptides while also stimulating ATPase activity, thereby mediating the refolding process and assisting Hsp70 in maintaining cellular proteostasis. Despite their importance, detailed structural information about JDP‒Hsp70 complexes is still being explored due to various technical challenges. One major challenge is the lack of more detailed structural data on full-length JDPs. Class A and B JDPs, the most extensively studied, are typically dimers of 300-400 residue polypeptides with central intrinsically disordered regions. These features complicate structural analysis via NMR and X-ray crystallography techniques. This work presents the 1H, 15N, and 13C backbone resonance assignments of the full-length (352 residues long) Sis1, a dimeric class B JDP from S. cerevisiae. Our study achieved 70.5% residue assignment distributed across the entire protein, providing probes in all Sis1 domains for the first time. To overcome this challenging task, strategies such as deuteration and 3D BEST-TROSY correlation experiments were used. The methods and results are detailed within the text. We are confident that this achievement will significantly benefit both the structural biology and the proteostasis scientific communities.","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":" ","pages":""},"PeriodicalIF":0.8,"publicationDate":"2024-12-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142908932","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

Correction: ¹H, ¹³C, and ¹⁵N resonance assignments of the amyloidogenic peptide SEM2(49-107) by NMR spectroscopy. 修正：核磁共振波谱对淀粉样蛋白肽SEM2（49-107）的1H， 13C和15N共振分配。

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2024-12-27 DOI: 10.1007/s12104-024-10214-1

Anastasia A Troshkina, Vladimir V Klochkov, Aydar G Bikmullin, Evelina A Klochkova, Dmitriy S Blokhin

引用次数: 0

¹H, ¹³C, and ¹⁵N resonance assignments of the amyloidogenic peptide SEM2(49-107) by NMR spectroscopy. 淀粉样蛋白肽SEM2（49-107）的1H， 13C和15N共振分配。

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2024-11-29 DOI: 10.1007/s12104-024-10209-y

Anastasia A Troshkina, Vladimir V Klochkov, Aydar G Bikmullin, Evelina A Klochkova, Dmitriy S Blokhin

{"title":"1H, 13C, and 15N resonance assignments of the amyloidogenic peptide SEM2(49-107) by NMR spectroscopy.","authors":"Anastasia A Troshkina, Vladimir V Klochkov, Aydar G Bikmullin, Evelina A Klochkova, Dmitriy S Blokhin","doi":"10.1007/s12104-024-10209-y","DOIUrl":"10.1007/s12104-024-10209-y","url":null,"abstract":"It has been shown that human seminal fluid is a major factor in enhancing HIV activity. The SEM2(49-107) peptide is a product of cleavage after ejaculation by internal prostheses of the semenogelin 2 protein, expressed in seminal vesicles. It is established that the peptide SEM2(49-107) forms amyloid fibrils, which increase probability of contracting HIV infection. In this nuclear magnetic resonance (NMR) study, we present almost complete (86%) resonance assignments for the 1H 15N and 13C atoms of the backbone and side-chain of the SEM2(49-107) peptide (BioMagResBank accession number 52356). The secondary structure of SEM2(49-107) peptide was estimated by using two approaches, secondary chemical shifts analysis (CSI) and TALOS-N prediction. Analysis of the secondary structure of the SEM2(49-107) peptide using both methods revealed that the peptide contains helical segments at the C-terminus. Also in this work, we used phase-sensitive 2D HSQC 1H- 15N experiments measuring longitudinal T1 and transverse T2 NMR relaxation times to report predicted secondary structure and backbone dynamics of the SEM2(49-107) peptide. This resonance assignment will form the basis of future NMR research, contributing to a better understanding of the peptide structure and internal dynamics of the molecule.","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":" ","pages":""},"PeriodicalIF":0.8,"publicationDate":"2024-11-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142749710","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