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

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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

Keywords

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

ASJC Scopus subject areas

  • Bioengineering
  • Biochemistry
  • Applied Microbiology and Biotechnology

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  • Cite this

    Yeo, K. J., Lee, W. C., Lee, S., Hwang, E., Park, J. S., Choi, I-G., Kim, S. I., Lee, J. C., Jeon, Y. H., Cheong, C., & Kim, H. Y. (2017). D-Stereoisomer preference of the OmpA-like domain of Pal in peptidoglycan of Acinetobacter baumannii. Process Biochemistry, 55, 110-115. https://doi.org/10.1016/j.procbio.2017.01.009