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基于β-内酰胺酶/转肽酶样超家族蛋白质结构催化核心比较的α和ω分类

Alpha and Omega Classification of β-Lactamase/Transpeptidase-like Superfamily Proteins Based on the Comparison of Their Structural Catalytic Cores.

作者信息

Denesyuk Alexander I, Denessiouk Konstantin, Johnson Mark S, Uversky Vladimir N

机构信息

Structural Bioinformatics Laboratory, Biochemistry, InFLAMES Research Flagship Center, Faculty of Science and Engineering, Åbo Akademi University, 20520 Turku, Finland.

Department of Molecular Medicine and USF Health Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL 33612, USA.

出版信息

Molecules. 2025 Apr 30;30(9):2019. doi: 10.3390/molecules30092019.

DOI:10.3390/molecules30092019
PMID:40363824
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC12073871/
Abstract

β-Lactamase/transpeptidase-like superfamily proteins are serine proteases that use the Ser-Lys catalytic dyad to carry out their biological functions. Here, we investigate the three known families of β-lactamase/transpeptidase-like superfamily proteins, β-lactamase/D-Ala carboxypeptidase, glutaminase, and Dac-like, and describe the structural catalytic cores that govern the catalytic residues in these proteins. We show that the structural catalytic core of these proteins is a combination of three zones, the mutual three-dimensional arrangement of which correspondingly determines their belonging to one of seven and twenty-four established groups and subgroups.

摘要

β-内酰胺酶/转肽酶样超家族蛋白是丝氨酸蛋白酶,利用丝氨酸-赖氨酸催化二元体来执行其生物学功能。在此,我们研究了β-内酰胺酶/转肽酶样超家族蛋白的三个已知家族,即β-内酰胺酶/D-丙氨酸羧肽酶、谷氨酰胺酶和类Dac蛋白,并描述了控制这些蛋白中催化残基的结构催化核心。我们表明,这些蛋白的结构催化核心是三个区域的组合,它们的相互三维排列相应地决定了它们属于七个既定组和二十四个亚组中的哪一组。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/28df/12073871/7f2883a98887/molecules-30-02019-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/28df/12073871/379e224ae4bc/molecules-30-02019-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/28df/12073871/44b731a84c41/molecules-30-02019-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/28df/12073871/999d8d77305f/molecules-30-02019-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/28df/12073871/7f2883a98887/molecules-30-02019-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/28df/12073871/379e224ae4bc/molecules-30-02019-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/28df/12073871/44b731a84c41/molecules-30-02019-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/28df/12073871/999d8d77305f/molecules-30-02019-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/28df/12073871/7f2883a98887/molecules-30-02019-g003.jpg

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本文引用的文献

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Int J Mol Sci. 2024 Nov 5;25(22):11858. doi: 10.3390/ijms252211858.
2
UniProt: the Universal Protein Knowledgebase in 2025.通用蛋白质知识库(UniProt):2025年的情况
Nucleic Acids Res. 2025 Jan 6;53(D1):D609-D617. doi: 10.1093/nar/gkae1010.
3
Frameshift Mutations in Genes Encoding PBP3 and PBP4 Trigger an Unusual, Extreme β-Lactam Resistance Phenotype in .
基因编码 PBP3 和 PBP4 的移码突变导致. 出现一种不寻常的、极端的β-内酰胺耐药表型
ACS Infect Dis. 2024 Nov 8;10(11):3810-3820. doi: 10.1021/acsinfecdis.4c00330. Epub 2024 Oct 23.
4
The active site of the SGNH hydrolase-like fold proteins: Nucleophile-oxyanion (Nuc-Oxy) and Acid-Base zones.SGNH水解酶样折叠蛋白的活性位点:亲核体-氧阴离子(Nuc-Oxy)区和酸碱区。
Curr Res Struct Biol. 2023 Dec 29;7:100123. doi: 10.1016/j.crstbi.2023.100123. eCollection 2024.
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Int J Mol Sci. 2023 Aug 24;24(17):13165. doi: 10.3390/ijms241713165.
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The ESTHER database on alpha/beta hydrolase fold proteins - An overview of recent developments.ESTHER 数据库中关于 α/β 水解酶折叠蛋白的概述——近期发展情况。
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Protein Sci. 2023 Jan;32(1):e4519. doi: 10.1002/pro.4519.
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