Structure-Function Characterization of the Conserved Regulatory Mechanism of the Escherichia coli M48 Metalloprotease BepA-Reference-Cited by-同舟云学术

Structure-Function Characterization of the Conserved Regulatory Mechanism of the Escherichia coli M48 Metalloprotease BepA

Published:2020-12-18 Issue:2 Volume:203 Page:
ISSN:0021-9193
Container-title:Journal of Bacteriology
language:en
Short-container-title:J Bacteriol

Author:

Bryant Jack A.¹,Cadby Ian T.¹,Chong Zhi-Soon²,Boelter Gabriela¹,Sevastsyanovich Yanina R.¹,Morris Faye C.¹^ORCID,Cunningham Adam F.¹^ORCID,Kritikos George¹,Meek Richard W.¹,Banzhaf Manuel¹,Chng Shu-Sin²^ORCID,Lovering Andrew L.¹,Henderson Ian R.¹³^ORCID

Affiliation:

1. Institute of Microbiology and Infection, University of Birmingham, Edgbaston, United Kingdom

2. Department of Chemistry, National University of Singapore, Singapore, Singapore

3. Institute for Molecular Bioscience, University of Queensland, St. Lucia, Australia

Abstract

M48 metalloproteases are widely distributed in all domains of life. E. coli possesses four members of this family located in multiple cellular compartments. The functions of these proteases are not well understood. Recent investigations revealed that one family member, BepA, has an important role in the maturation of a central component of the lipopolysaccharide (LPS) biogenesis machinery. Here, we present the structure of BepA and the results of a structure-guided mutagenesis strategy, which reveal the key residues required for activity that inform how all M48 metalloproteases function.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/JB.00434-20

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