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The structure of Rv3717 reveals a novel amidase from Mycobacterium tuberculosis

Bacterial N-acetylmuramoyl-l-alanine amidases are cell-wall hydrolases that hydrolyze the bond between N-acetylmuramic acid and l-alanine in cell-wall glycopeptides. Rv3717 of Mycobacterium tuberculosis has been identified as a unique autolysin that lacks a cell-wall-binding domain (CBD) and its str...

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Autores principales: Kumar, Atul, Kumar, Sanjiv, Kumar, Dilip, Mishra, Arpit, Dewangan, Rikeshwer P., Shrivastava, Priyanka, Ramachandran, Srinivasan, Taneja, Bhupesh
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3852659/
https://www.ncbi.nlm.nih.gov/pubmed/24311595
http://dx.doi.org/10.1107/S0907444913026371
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author Kumar, Atul
Kumar, Sanjiv
Kumar, Dilip
Mishra, Arpit
Dewangan, Rikeshwer P.
Shrivastava, Priyanka
Ramachandran, Srinivasan
Taneja, Bhupesh
author_facet Kumar, Atul
Kumar, Sanjiv
Kumar, Dilip
Mishra, Arpit
Dewangan, Rikeshwer P.
Shrivastava, Priyanka
Ramachandran, Srinivasan
Taneja, Bhupesh
author_sort Kumar, Atul
collection PubMed
description Bacterial N-acetylmuramoyl-l-alanine amidases are cell-wall hydrolases that hydrolyze the bond between N-acetylmuramic acid and l-alanine in cell-wall glycopeptides. Rv3717 of Mycobacterium tuberculosis has been identified as a unique autolysin that lacks a cell-wall-binding domain (CBD) and its structure has been determined to 1.7 Å resolution by the Pt-­SAD phasing method. Rv3717 possesses an α/β-fold and is a zinc-dependent hydrolase. The structure reveals a short flexible hairpin turn that partially occludes the active site and may be involved in autoregulation. This type of autoregulation of activity of PG hydrolases has been observed in Bartonella henselae amidase (AmiB) and may be a general mechanism used by some of the redundant amidases to regulate cell-wall hydrolase activity in bacteria. Rv3717 utilizes its net positive charge for substrate binding and exhibits activity towards a broad spectrum of substrate cell walls. The enzymatic activity of Rv3717 was confirmed by isolation and identification of its enzymatic products by LC/MS. These studies indicate that Rv3717, an N-acetylmuramoyl-l-alanine amidase from M. tuberculosis, represents a new family of lytic amidases that do not have a separate CBD and are regulated conformationally.
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spelling pubmed-38526592013-12-12 The structure of Rv3717 reveals a novel amidase from Mycobacterium tuberculosis Kumar, Atul Kumar, Sanjiv Kumar, Dilip Mishra, Arpit Dewangan, Rikeshwer P. Shrivastava, Priyanka Ramachandran, Srinivasan Taneja, Bhupesh Acta Crystallogr D Biol Crystallogr Research Papers Bacterial N-acetylmuramoyl-l-alanine amidases are cell-wall hydrolases that hydrolyze the bond between N-acetylmuramic acid and l-alanine in cell-wall glycopeptides. Rv3717 of Mycobacterium tuberculosis has been identified as a unique autolysin that lacks a cell-wall-binding domain (CBD) and its structure has been determined to 1.7 Å resolution by the Pt-­SAD phasing method. Rv3717 possesses an α/β-fold and is a zinc-dependent hydrolase. The structure reveals a short flexible hairpin turn that partially occludes the active site and may be involved in autoregulation. This type of autoregulation of activity of PG hydrolases has been observed in Bartonella henselae amidase (AmiB) and may be a general mechanism used by some of the redundant amidases to regulate cell-wall hydrolase activity in bacteria. Rv3717 utilizes its net positive charge for substrate binding and exhibits activity towards a broad spectrum of substrate cell walls. The enzymatic activity of Rv3717 was confirmed by isolation and identification of its enzymatic products by LC/MS. These studies indicate that Rv3717, an N-acetylmuramoyl-l-alanine amidase from M. tuberculosis, represents a new family of lytic amidases that do not have a separate CBD and are regulated conformationally. International Union of Crystallography 2013-12-01 2013-11-19 /pmc/articles/PMC3852659/ /pubmed/24311595 http://dx.doi.org/10.1107/S0907444913026371 Text en © Kumar et al. 2013 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.
spellingShingle Research Papers
Kumar, Atul
Kumar, Sanjiv
Kumar, Dilip
Mishra, Arpit
Dewangan, Rikeshwer P.
Shrivastava, Priyanka
Ramachandran, Srinivasan
Taneja, Bhupesh
The structure of Rv3717 reveals a novel amidase from Mycobacterium tuberculosis
title The structure of Rv3717 reveals a novel amidase from Mycobacterium tuberculosis
title_full The structure of Rv3717 reveals a novel amidase from Mycobacterium tuberculosis
title_fullStr The structure of Rv3717 reveals a novel amidase from Mycobacterium tuberculosis
title_full_unstemmed The structure of Rv3717 reveals a novel amidase from Mycobacterium tuberculosis
title_short The structure of Rv3717 reveals a novel amidase from Mycobacterium tuberculosis
title_sort structure of rv3717 reveals a novel amidase from mycobacterium tuberculosis
topic Research Papers
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3852659/
https://www.ncbi.nlm.nih.gov/pubmed/24311595
http://dx.doi.org/10.1107/S0907444913026371
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