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 journalArticlepeer-review

1 Citation (Scopus)


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
Publication statusPublished - 2017 Apr 1


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

ASJC Scopus subject areas

  • Bioengineering
  • Biochemistry
  • Applied Microbiology and Biotechnology


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