D-Stereoisomer preference of the OmpA-like domain of Pal in peptidoglycan of Acinetobacter baumannii

Kwon Joo Yeo, Woo Cheol Lee, Saeyoung Lee, Eunha Hwang, Jeong Soon Park, In-Geol Choi, Seung Il Kim, Je Chul Lee, Young Ho Jeon, Chaejoon Cheong, Hye Yeon Kim

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

OmpA-like domain proteins bind to peptidoglycan by interacting with the D-amino acid moiety of meso-diaminopimelate in peptidoglycan, but it is still not clear how this domain recognizes the D-amino region of peptidoglycan. To study their D-stereoisomer preference, we solved the crystal structures of the OmpA-like domains of Acinetobacter baumannii peptidoglycan-associated lipoprotein (AbPal) in complex with D- or L-diaminopimelate. Our results reveal that these domains can bind both enantiomers of diaminopimelate with a greater affinity for D-diaminopimelate. The crystal structures of wild-type AbPal in complex with meso-diaminopimelate and mutant AbPal in complete with the LL-diaminopimelate ligand suggests that the Tyr85 residue of AbPal is an important determinant for this D-amino acid moiety preference. Our findings provide a basis for the development of antibacterial agents that inhibit interactions between PGN and OmpA-like domains and disrupt the stability of cell walls of gram-negative bacteria.

Original languageEnglish
Pages (from-to)110-115
Number of pages6
JournalProcess Biochemistry
Volume55
DOIs
Publication statusPublished - 2017 Apr 1

Fingerprint

Lipoproteins
Acinetobacter baumannii
Stereoisomerism
Peptidoglycan
Amino acids
Crystal structure
Bactericides
Enantiomers
Bacteria
Ligands
Amino Acids
Cells
Proteins
Gram-Negative Bacteria
Cell Wall
Anti-Bacterial Agents

Keywords

  • AbPal
  • Diaminopimelate
  • OmpA-like domain
  • Peptidoglycan
  • Peptidoglycan-associated lipoprotein

ASJC Scopus subject areas

  • Bioengineering
  • Biochemistry
  • Applied Microbiology and Biotechnology

Cite this

D-Stereoisomer preference of the OmpA-like domain of Pal in peptidoglycan of Acinetobacter baumannii. / Yeo, Kwon Joo; Lee, Woo Cheol; Lee, Saeyoung; Hwang, Eunha; Park, Jeong Soon; Choi, In-Geol; Kim, Seung Il; Lee, Je Chul; Jeon, Young Ho; Cheong, Chaejoon; Kim, Hye Yeon.

In: Process Biochemistry, Vol. 55, 01.04.2017, p. 110-115.

Research output: Contribution to journalArticle

Yeo, KJ, Lee, WC, Lee, S, Hwang, E, Park, JS, Choi, I-G, Kim, SI, Lee, JC, Jeon, YH, Cheong, C & Kim, HY 2017, 'D-Stereoisomer preference of the OmpA-like domain of Pal in peptidoglycan of Acinetobacter baumannii', Process Biochemistry, vol. 55, pp. 110-115. https://doi.org/10.1016/j.procbio.2017.01.009
Yeo, Kwon Joo ; Lee, Woo Cheol ; Lee, Saeyoung ; Hwang, Eunha ; Park, Jeong Soon ; Choi, In-Geol ; Kim, Seung Il ; Lee, Je Chul ; Jeon, Young Ho ; Cheong, Chaejoon ; Kim, Hye Yeon. / D-Stereoisomer preference of the OmpA-like domain of Pal in peptidoglycan of Acinetobacter baumannii. In: Process Biochemistry. 2017 ; Vol. 55. pp. 110-115.
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