Biomolecular NMR Assignments最新文献_第7页

1H, 13C, 15N backbone resonance assignment of Escherichia coli adenylate kinase 大肠杆菌腺苷酸激酶的1H，13C，15N骨架共振定位

IF 0.9 4区生物学

Biomolecular NMR Assignments Pub Date : 2023-08-26 DOI: 10.1007/s12104-023-10147-1

Julia A. Brom, Sasiprapa Samsri, Ruta G. Petrikis, Stuart Parnham, Gary J. Pielak

引用次数: 0

Backbone and sidechain NMR assignments of residues 1–81 from yeast Sis1 in complex with an Hsp70 C-terminal EEVD peptide 酵母Sis1与Hsp70 c端EEVD肽复合物中残基1-81的主链和侧链NMR定位。

IF 0.9 4区生物学

Biomolecular NMR Assignments Pub Date : 2023-08-17 DOI: 10.1007/s12104-023-10148-0

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

引用次数: 0

1H, 15N and 13C backbone and side chain solution NMR assignments of the TPM domain-containing protein of the thermophilic bacterium Rhodothermus marinus 嗜热细菌Rhodothermus marinus的含TPM结构域蛋白质的1H、15N和13C主链和侧链溶液NMR归属

IF 0.9 4区生物学

Biomolecular NMR Assignments Pub Date : 2023-08-05 DOI: 10.1007/s12104-023-10146-2

Leonardo Pellizza, Lila Ramis, Ignacio Argañaraz Araoz, Martín Aran

{"title":"1H, 15N and 13C backbone and side chain solution NMR assignments of the TPM domain-containing protein of the thermophilic bacterium Rhodothermus marinus","authors":"Leonardo Pellizza, Lila Ramis, Ignacio Argañaraz Araoz, Martín Aran","doi":"10.1007/s12104-023-10146-2","DOIUrl":"10.1007/s12104-023-10146-2","url":null,"abstract":"<div><p>The InterPro family IPR007621 TPM_phosphatase is a widely conserved family of protein domains found in prokaryotes, plants and invertebrates. Despite similar predicted protein folding, members of this family are involved in different cellular processes. In recent years, the structural and biochemical characterization of evolutionarily divergent TPM domains has shown their ability to hydrolyze phosphate groups of different substrates. However, there are still inaccurate functional annotations and uncertain relationships between the structure and function of this domain family. We here report the <sup>1</sup>H, <sup>13</sup>C, and <sup>15</sup>N backbone and sidechain resonances of the TPM domain of a predicted TPM domain-containing protein of the thermophilic bacterium <i>Rhodothermus marinus</i>. These data will lay the groundwork for future NMR-based investigations, contributing to a thorough comprehension of the intricate aspects governing the interplay between structure and function of TPM domains. Additionally, they will unlock opportunities to explore dynamic structural changes, providing valuable insights into the molecular mechanisms underlying the evolutionary adaptations to extreme environmental conditions within this protein family.</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"17 2","pages":"229 - 233"},"PeriodicalIF":0.9,"publicationDate":"2023-08-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71909141","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 and side chain NMR assignments and secondary structure calculation of the pheromone binding protein3 of Ostrinia nubilalis, an agricultural pest 农业害虫nubilalis Ostrinia nubilalis信息素结合蛋白3的主侧链NMR定位和二级结构计算。

IF 0.9 4区生物学

Biomolecular NMR Assignments Pub Date : 2023-07-27 DOI: 10.1007/s12104-023-10145-3

Omar Al-Danoon, Smita Mohanty

{"title":"Backbone and side chain NMR assignments and secondary structure calculation of the pheromone binding protein3 of Ostrinia nubilalis, an agricultural pest","authors":"Omar Al-Danoon, Smita Mohanty","doi":"10.1007/s12104-023-10145-3","DOIUrl":"10.1007/s12104-023-10145-3","url":null,"abstract":"<div><p><i>Ostrinia nubilalis</i>, also known as European Corn Borer (ECB), is a serious pest in Europe and North America, as well as in Central Asia and Northern Africa. It damages a variety of agricultural crops such as corn, oats, buckwheat, millet, and soybeans. causing annually at least one billion dollars in loss. The <i>Ostrinia nubilalis</i> pheromone-binding protein3 (OnubPBP3), preferentially expressed in the male moth antenna, has been implicated in the detection of the female-secreted pheromone blend during the mating process. Understanding the structure of and function of OnubPBP3, including the mechanism of pheromone binding and its release at the dendritic olfactory neuron (ORN), is essential if integrated pest management through sensory inhibition is to be achieved. We report here the backbone and side-chain resonance assignments of OnubPBP3 at pH 6.5 using various triple resonance NMR experiments on a <sup>13</sup>C, <sup>15</sup>N-labeled protein sample. The secondary structure of OnubPBP3 consists of six α-helices and an unstructured C-terminus based on backbone chemical shifts.</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"17 2","pages":"223 - 227"},"PeriodicalIF":0.9,"publicationDate":"2023-07-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9879801","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 and 15N backbone and side-chain resonance assignments of ∆∆BmSA1, the surface antigen of Babesia microti 微巴贝斯虫表面抗原∆∆BmSA1的1H、13C和15N主链和侧链共振分配

IF 0.9 4区生物学

Biomolecular NMR Assignments Pub Date : 2023-07-15 DOI: 10.1007/s12104-023-10144-4

Assia Mouhand, Joana Pissarra, Stéphane Delbecq, Christian Roumestand, Philippe Barthe

{"title":"1H, 13C and 15N backbone and side-chain resonance assignments of ∆∆BmSA1, the surface antigen of Babesia microti","authors":"Assia Mouhand, Joana Pissarra, Stéphane Delbecq, Christian Roumestand, Philippe Barthe","doi":"10.1007/s12104-023-10144-4","DOIUrl":"10.1007/s12104-023-10144-4","url":null,"abstract":"<div><p>Human babesiosis is a vector-borne zoonotic infection caused mostly by the Apicomplexan parasite <i>Babesia microti</i>, distributed worldwide. The infection can result in severe symptoms such as hemolytic anemia, especially in immunodeficient patients. Also, asymptomatic patients continue transmission as unscreened blood donors, and represent a risk for Public Health. Early host-parasite interactions are mediated by BmSA1, the major surface antigen of <i>Babesia microti</i>, crucial for invasion and immune escape. Hence, a structural and functional characterization of the BmSA1 protein constitutes a first strategic milestone toward the development of innovative tools to control infection. Knowledge of the 3D structure of such an important antigen is crucial for the development of vaccines or new diagnostic tests. Here, we report the <sup>1</sup>H, <sup>15</sup>N and <sup>13</sup>C NMR resonance assignment of ∆∆BmSA1, a truncated recombinant version of BmSA1 without the N-terminal signal peptide and the hydrophobic C-terminal GPI-anchor. Secondary structure prediction using CSI.3 and TALOS-N demonstrates a high content of alpha-helical structure. This preliminary study provides foundations for further structural characterization of BMSA1.</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"17 2","pages":"217 - 221"},"PeriodicalIF":0.9,"publicationDate":"2023-07-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71909559","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 1H, 13C and 15N assignments of the apo-acyl carrier protein (ACP1) of Pseudomonas aeruginosa 铜绿假单胞菌载脂蛋白载体蛋白(ACP1)骨架1H, 13C和15N的分配

IF 0.9 4区生物学

Biomolecular NMR Assignments Pub Date : 2023-07-08 DOI: 10.1007/s12104-023-10138-2

Madison Rizzo, Eric Baggs, Abu Sayeed Chowdhury, Rajesh Nagarajan, Lisa Rose Warner

引用次数: 0

Chemical shift assignments of dsRBD1 and linker region of R2D2, a siRNA binding protein in the Drosophila RNAi pathway 果蝇RNAi通路中siRNA结合蛋白dsRBD1和R2D2连接区域的化学位移定位。

IF 0.9 4区生物学

Biomolecular NMR Assignments Pub Date : 2023-07-05 DOI: 10.1007/s12104-023-10143-5

Ramdas Aute, Mandar V. Deshmukh

引用次数: 0

Backbone 1H, 15N and 13C resonance assignments for dengue NS2B without the NS3 protease cofactor region in detergent micelles 洗涤剂胶束中不含NS3蛋白酶辅因子区的登革NS2B的主链1H、15N和13C共振分配

IF 0.9 4区生物学

Biomolecular NMR Assignments Pub Date : 2023-07-05 DOI: 10.1007/s12104-023-10142-6

Qingxin Li, Hui Qi Ng, Ying Ru Loh, CongBao Kang

{"title":"Backbone 1H, 15N and 13C resonance assignments for dengue NS2B without the NS3 protease cofactor region in detergent micelles","authors":"Qingxin Li, Hui Qi Ng, Ying Ru Loh, CongBao Kang","doi":"10.1007/s12104-023-10142-6","DOIUrl":"10.1007/s12104-023-10142-6","url":null,"abstract":"<div><p>Dengue virus is an important human pathogen affecting people especially in tropical and subtropical regions. Its genome encodes seven non-structural proteins that are important for viral assembly and replication. Dengue NS2B is a membrane protein containing four transmembrane helices and involved in protein-protein interactions. Its transmembrane helices are critical for location of NS2B on the cell membrane while one cytoplasmic region composed of approximately 40 amino acids serves as a cofactor of viral NS3 protease by forming a tight complex with the N-terminal region of NS3. Here, we report the backbone resonance assignments for a dengue NS2B construct referred to as mini-NS2B containing only the transmembrane regions without NS3 cofactor region in detergent micelles. Mini-NS2B exhibits well-dispersed cross-peaks in the <sup>1</sup>H-<sup>15</sup>N-HSQC spectrum and contains four helices in solution. The available mini-NS2B and its assignment will be useful for determining the structure of NS2B and identifying small molecules binding to the transmembrane regions.</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"17 2","pages":"205 - 209"},"PeriodicalIF":0.9,"publicationDate":"2023-07-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71908985","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, and 15N resonance assignments of SarA monomer from Staphylococcus aureus in complex with DNA 金黄色葡萄球菌SarA单体与DNA复合物的1H、13C和15N共振归属

IF 0.9 4区生物学

Biomolecular NMR Assignments Pub Date : 2023-07-05 DOI: 10.1007/s12104-023-10140-8

Dihong Fu, Bo Duan, Xianzhi Dong, Bin Xia

引用次数: 0

Resonance assignments of the PUB domain of the RNF31 protein RNF31蛋白PUB结构域的共振配位。

IF 0.9 4区生物学

Biomolecular NMR Assignments Pub Date : 2023-07-03 DOI: 10.1007/s12104-023-10139-1

Lanlan Song, Fumei Zhong, Xiaoming Tu, Jiahai Zhang

引用次数: 0