Biomolecular NMR Assignments最新文献

Backbone resonance assignments of PhoCl, a photocleavable protein. PhoCl蛋白的主链共振配位。

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2025-01-18 DOI: 10.1007/s12104-025-10215-8

Runhan Wang, Lina Zhu, Junfeng Wang, Lei Zhu

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

NMR resonance assignment of a ligand-binding domain of ephrin receptor A2. ephrin受体A2配体结合域的核磁共振配位。

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2024-12-19 DOI: 10.1007/s12104-024-10211-4

Konstantin S Mineev, Santosh L Gande, Verena Linhard, Sattar Khashkhashi Moghaddam, Harald Schwalbe

引用次数: 0

Backbone resonance assignments of the C-terminal thioesterase domain of tyrocidine synthetase C. 酪氨酸合成酶C-末端硫酯酶结构域的主链共振配位。

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2024-12-11 DOI: 10.1007/s12104-024-10210-5

Mitsuhiro Takeda, Rino Saito, Sho Konno, Takayuki Nagae, Hiroshi Aoyama, Sosuke Yoshinaga, Hiroaki Terasawa, Akihiro Taguchi, Atsuhiko Taniguchi, Yoshio Hayashi, Masaki Mishima

{"title":"Backbone resonance assignments of the C-terminal thioesterase domain of tyrocidine synthetase C.","authors":"Mitsuhiro Takeda, Rino Saito, Sho Konno, Takayuki Nagae, Hiroshi Aoyama, Sosuke Yoshinaga, Hiroaki Terasawa, Akihiro Taguchi, Atsuhiko Taniguchi, Yoshio Hayashi, Masaki Mishima","doi":"10.1007/s12104-024-10210-5","DOIUrl":"https://doi.org/10.1007/s12104-024-10210-5","url":null,"abstract":"Natural macrocyclic peptides produced by microorganisms serve as valuable resources for therapeutic compounds, including antibiotics, anticancer agents, and immune suppressive agents. Nonribosomal peptide synthetases (NRPSs) are responsible for the biosynthesis of macrocyclic peptides. NRPSs are large multimodular enzymes, and each module recognizes and incorporates one specific amino acid into the polypeptide product. In the final biosynthetic step, the mature linear peptide precursor is subject to head-to-tail cyclization by the thioesterase (TE) domain in the C-terminal module. Since the TE domains can autonomously catalyze the cyclization of diverse linear peptide substrates, isolated TE domains can be used to produce natural product derivatives. To understand the mechanism of TE domains in NRPSs as a base for therapeutic applications, we investigated the TE domain (residues 6236-6486) of tyrocidine synthetase TycC by NMR. Tyrocidine is a cyclic decapeptide with antibiotic activity, and TycC-TE catalyzes the cyclization of the linear decapeptide precursor. Here, we report the backbone resonance assignments of TycC-TE. The assignments of TycC-TE provide the basis for NMR investigations of the structure and substrate-recognition mode of the TE domain in NRPS.","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":" ","pages":""},"PeriodicalIF":0.8,"publicationDate":"2024-12-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142805711","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 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

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 : 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

Backbone 1H, 15N, and 13C resonance assignments of the FF1 domain from P190A RhoGAP in 5 and 8 M urea P190A RhoGAP 的 FF1 结构域在 5 M 和 8 M 尿素中的 1H、15N 和 13C 骨架共振赋值。

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2024-10-14 DOI: 10.1007/s12104-024-10197-z

Aarão Camilo-Ramos, Dmitry M. Korzhnev, Ramon Pinheiro-Aguiar, Fabio C. L. Almeida

引用次数: 0