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Structure. 2016 Dec 6;24(12):2227-2235. doi: 10.1016/j.str.2016.10.009. Epub 2016 Nov 17.

OmpA: A Flexible Clamp for Bacterial Cell Wall Attachment.

Author information

1
School of Chemistry, University of Southampton, Highfield, Southampton SO17 1BJ, UK.
2
School of Chemistry, University of Southampton, Highfield, Southampton SO17 1BJ, UK; CBR Division, Defence Science and Technology Laboratory, Porton Down, Salisbury, Wiltshire SP4 0JQ, UK.
3
Bioinformatics Institute (A(∗)STAR), 30 Biopolis Street, 07-01 Matrix, Singapore 138671, Singapore; National University of Singapore, Department of Biological Sciences, 14 Science Drive 4, Singapore 117543, Singapore. Electronic address: peterjb@bii.a-star.edu.sg.
4
School of Chemistry, University of Southampton, Highfield, Southampton SO17 1BJ, UK. Electronic address: s.khalid@soton.ac.uk.

Abstract

The envelope of Gram-negative bacteria is highly complex, containing separate outer and inner membranes and an intervening periplasmic space encompassing a peptidoglycan (PGN) cell wall. The PGN scaffold is anchored non-covalently to the outer membrane via globular OmpA-like domains of various proteins. We report atomically detailed simulations of PGN bound to OmpA in three different states, including the isolated C-terminal domain (CTD), the full-length monomer, or the complete full-length dimeric form. Comparative analysis of dynamics of OmpA CTD from different bacteria helped to identify a conserved PGN-binding mode. The dynamics of full-length OmpA, embedded within a realistic representation of the outer membrane containing full-rough (Ra) lipopolysaccharide, phospholipids, and cardiolipin, suggested how the protein may provide flexible mechanical support to the cell wall. An accurate model of the heterogeneous bacterial cell envelope should facilitate future efforts to develop antibacterial agents.

KEYWORDS:

Escherichia coli; OmpA; bacterial cell envelope; cell wall; molecular dynamics; outer membrane; peptidoglycan; simulation

PMID:
27866852
DOI:
10.1016/j.str.2016.10.009
[Indexed for MEDLINE]
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