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本文引用的文献

1
Atomic resolution structures of CTX-M beta-lactamases: extended spectrum activities from increased mobility and decreased stability.CTX-M β-内酰胺酶的原子分辨率结构：因流动性增加和稳定性降低而具有的超广谱活性
J Mol Biol. 2005 Apr 29;348(2):349-62. doi: 10.1016/j.jmb.2005.02.010.
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Coot: model-building tools for molecular graphics.Coot：分子图形的模型构建工具。
Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2126-32. doi: 10.1107/S0907444904019158. Epub 2004 Nov 26.
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The CCP4 suite: programs for protein crystallography.CCP4软件包：用于蛋白质晶体学的程序。
Acta Crystallogr D Biol Crystallogr. 1994 Sep 1;50(Pt 5):760-3. doi: 10.1107/S0907444994003112.
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Growing group of extended-spectrum beta-lactamases: the CTX-M enzymes.超广谱β-内酰胺酶的不断增长的群体：CTX-M酶。
Antimicrob Agents Chemother. 2004 Jan;48(1):1-14. doi: 10.1128/AAC.48.1.1-14.2004.
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Crystal structure of extended-spectrum beta-lactamase Toho-1: insights into the molecular mechanism for catalytic reaction and substrate specificity expansion.超广谱β-内酰胺酶Toho-1的晶体结构：对催化反应和底物特异性扩展分子机制的见解
Biochemistry. 2003 Sep 16;42(36):10634-43. doi: 10.1021/bi0342822.
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Understanding the acylation mechanisms of active-site serine penicillin-recognizing proteins: a molecular dynamics simulation study.理解活性位点丝氨酸青霉素识别蛋白的酰化机制：分子动力学模拟研究
Proteins. 2003 Oct 1;53(1):88-100. doi: 10.1002/prot.10450.
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Post surgical atypical mycobacterial infection due to Mycobacterium fortuitum.手术后由偶然分枝杆菌引起的非典型分枝杆菌感染。
J Infect. 2002 Oct;45(3):210-11. doi: 10.1016/s0163-4453(02)91033-9.
8
Acyl-intermediate structures of the extended-spectrum class A beta-lactamase, Toho-1, in complex with cefotaxime, cephalothin, and benzylpenicillin.超广谱A类β-内酰胺酶Toho-1与头孢噻肟、头孢菌素和苄青霉素复合物的酰基中间体结构。
J Biol Chem. 2002 Nov 29;277(48):46601-8. doi: 10.1074/jbc.M207884200. Epub 2002 Sep 8.
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Structure of an extended-spectrum class A beta-lactamase from Proteus vulgaris K1.
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10
Crystal structures of the Bacillus licheniformis BS3 class A beta-lactamase and of the acyl-enzyme adduct formed with cefoxitin.地衣芽孢杆菌BS3 A类β-内酰胺酶及其与头孢西丁形成的酰基酶加合物的晶体结构。
Biochemistry. 2002 Feb 12;41(6):1877-85. doi: 10.1021/bi015789k.

偶然分枝杆菌A类β-内酰胺酶的晶体结构：广泛底物特异性的结构基础

Crystal structure of the Mycobacterium fortuitum class A beta-lactamase: structural basis for broad substrate specificity.

作者信息

Sauvage Eric, Fonzé Eveline, Quinting Birgit, Galleni Moreno, Frère Jean-Marie, Charlier Paulette

机构信息

Centre d'Ingénierie des Protéines, Université de Liège, Institut de Physique B5, B-4000 Liège, Belgium.

出版信息

Antimicrob Agents Chemother. 2006 Jul;50(7):2516-21. doi: 10.1128/AAC.01226-05.

DOI:10.1128/AAC.01226-05
PMID:16801434
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1489783/
Abstract

beta-Lactamases are the main cause of bacterial resistance to penicillins and cephalosporins. Class A beta-lactamases, the largest group of beta-lactamases, have been found in many bacterial strains, including mycobacteria, for which no beta-lactamase structure has been previously reported. The crystal structure of the class A beta-lactamase from Mycobacterium fortuitum (MFO) has been solved at 2.13-A resolution. The enzyme is a chromosomally encoded broad-spectrum beta-lactamase with low specific activity on cefotaxime. Specific features of the active site of the class A beta-lactamase from M. fortuitum are consistent with its specificity profile. Arg278 and Ser237 favor cephalosporinase activity and could explain its broad substrate activity. The MFO active site presents similarities with the CTX-M type extended-spectrum beta-lactamases but lacks a specific feature of these enzymes, the VNYN motif (residues 103 to 106), which confers on CTX-M-type extended-spectrum beta-lactamases a more efficient cefotaximase activity.

摘要

β-内酰胺酶是细菌对青霉素和头孢菌素耐药的主要原因。A类β-内酰胺酶是β-内酰胺酶中最大的一组，已在许多细菌菌株中发现，包括分枝杆菌，此前尚未报道过其β-内酰胺酶结构。偶然分枝杆菌（MFO）的A类β-内酰胺酶的晶体结构已在2.13埃分辨率下解析。该酶是一种染色体编码的广谱β-内酰胺酶，对头孢噻肟的比活性较低。偶然分枝杆菌A类β-内酰胺酶活性位点的特定特征与其特异性谱一致。Arg278和Ser237有利于头孢菌素酶活性，并可解释其广泛的底物活性。MFO活性位点与CTX-M型超广谱β-内酰胺酶有相似之处，但缺乏这些酶的一个特定特征，即VNYN基序（第103至106位残基），该基序赋予CTX-M型超广谱β-内酰胺酶更有效的头孢噻肟酶活性。