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

Authors
Yeo, Kwon JooLee, Woo CheolLee, SaeyoungHwang, EunhaPark, Jeong SoonChoi, In-GeolKim, Seung IlLee, Je ChulJeon, Young HoCheong, ChaejoonKim, Hye-Yeon
Issue Date
4월-2017
Publisher
ELSEVIER SCI LTD
Keywords
Peptidoglycan-associated lipoprotein; OmpA-like domain; Peptidoglycan Diaminopimelate; AbPal
Citation
PROCESS BIOCHEMISTRY, v.55, pp.110 - 115
Indexed
SCIE
SCOPUS
Journal Title
PROCESS BIOCHEMISTRY
Volume
55
Start Page
110
End Page
115
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/83813
DOI
10.1016/j.procbio.2017.01.009
ISSN
1359-5113
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. (C) 2017 Elsevier Ltd. All rights reserved.
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