Editing Beta-lactamase (section)

== Structure ==

The structure of a ''[[Streptomyces]]'' serine β-lactamase (SBLs) is given by {{PDB link|1BSG}}. The alpha-beta fold ({{InterPro|IPR012338}}) resembles that of a [[DD-Transpeptidase|<small>DD</small>-transpeptidase]], from which the enzyme is thought to have evolved. β-lactam antibiotics bind to <small>DD</small>-transpeptidases to inhibit bacterial cell wall biosynthesis. Serine β-lactamases are grouped by sequence similarity into types A, C, and D.

The other type of beta-lactamase is of the metallo type ("type B"). Metallo-beta-lactamases (MBLs) need metal ion(s) (1 or 2 Zn<sup>2+</sup> ions<ref name=":0">{{cite journal | vauthors = Rotondo CM, Wright GD | title = Inhibitors of metallo-β-lactamases | journal = Current Opinion in Microbiology | volume = 39 | pages = 96–105 | date = October 2017 | pmid = 29154026 | doi = 10.1016/j.mib.2017.10.026 }}</ref>) on their active site for their catalytic activities.<ref>{{cite journal | vauthors = Shi C, Chen J, Kang X, Shen X, Lao X, Zheng H | title = Approaches for the discovery of metallo-β-lactamase inhibitors: A review | journal = Chemical Biology & Drug Design | volume = 94 | issue = 2 | pages = 1427–1440 | date = August 2019 | pmid = 30925023 | doi = 10.1111/cbdd.13526 | s2cid = 85566136 }}</ref> The structure of the [[New Delhi metallo-beta-lactamase 1]] is given by {{PDB link|6C89}}. It resembles a [[RNase Z]], from which it is thought to have evolved.