d-Stereoisomer preference of the OmpA-like domain of Pal in peptidoglycan of Acinetobacter baumannii
| Autor: | In Geol Choi, Je Chul Lee, Kwon Joo Yeo, Saeyoung Lee, Woo Cheol Lee, Hye-Yeon Kim, Seung Il Kim, Eunha Hwang, Young Ho Jeon, Chaejoon Cheong, Jeong Soon Park |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
chemistry.chemical_classification 030106 microbiology Mutant Pseudopeptidoglycan Bioengineering Biology Ligand (biochemistry) Applied Microbiology and Biotechnology Biochemistry Amino acid carbohydrates (lipids) Cell wall 03 medical and health sciences chemistry.chemical_compound Residue (chemistry) 030104 developmental biology chemistry Moiety Peptidoglycan |
| Zdroj: | Process Biochemistry. 55:110-115 |
| ISSN: | 1359-5113 |
| Popis: | 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 l l -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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect