6a6a | pdb_00006a6a

VanYB in complex with D-Alanine

spinqualitylabelsall models 6a6a, resolution 2.26Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6a6a is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT, DAL, GOL, PGE, ZN Activity: Serine-type D-Ala-D-Ala carboxypeptidase, with EC number 3.4.16.4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [VANY_ENTFA] Vancomycin-inducible, penicillin-resistant, DD-carboxypeptidase that hydrolyzes depsipeptide- and D-alanyl-D-alanine-containing peptidoglycan precursors. Insensitive to beta-lactams. Publication Abstract from PubMed Vancomycin resistance in Enterococci and its transfer to methicillin-resistant Staphylococcus aureus are challenging problems in health care institutions worldwide. High-level vancomycin resistance is conferred by acquiring either transposable elements of the VanA or VanB type. Enterococcus faecalis VanYB in the VanB-type operon is a d,d-carboxypeptidase that recognizes the peptidyl-d-Ala(4)-d-Ala(5) extremity of peptidoglycan and hydrolyses the terminal d-Ala on the extracellular side of the cell wall, thereby increasing the level of glycopeptide antibiotics resistance. However, at the molecular level, it remains unclear how VanYB manipulates peptidoglycan peptides for vancomycin resistance. In this study, we have determined the crystal structures of E. faecalis VanYB in the d-Ala-d-Ala-bound, d-Ala-bound, and -unbound states. The interactions between VanYB and d-Ala-d-Ala observed in the crystal provide the molecular basis for the recognition of peptidoglycan substrates by VanYB. Moreover, comparisons with the related VanX and VanXY enzymes reveal distinct structural features of E. faecalis VanYB around the active-site cleft, thus shedding light on its unique substrate specificity. Our results could serve as the foundation for unravelling the molecular mechanism of vancomycin resistance and for developing novel antibiotics against the vancomycin-resistant Enterococcus species. Structural basis for the substrate recognition of peptidoglycan pentapeptides by Enterococcus faecalis VanYB.,Kim HS, Hahn H, Kim J, Jang DM, Lee JY, Back JM, Im HN, Kim H, Han BW, Suh SW Int J Biol Macromol. 2018 Jul 27;119:335-344. doi:, 10.1016/j.ijbiomac.2018.07.081. PMID:30016658 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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