1R44
Crystal Structure of VanX
Summary for 1R44
| Entry DOI | 10.2210/pdb1r44/pdb |
| Descriptor | D-alanyl-D-alanine dipeptidase, ZINC ION (3 entities in total) |
| Functional Keywords | vanx, e.faecium, dipeptidase, hydrolase |
| Biological source | Enterococcus faecium |
| Total number of polymer chains | 6 |
| Total formula weight | 140841.46 |
| Authors | Pratt, S.D.,Katz, L.,Severin, J.M.,Holzman, T.,Park, C.H. (deposition date: 2003-10-03, release date: 2004-06-15, Last modification date: 2024-02-14) |
| Primary citation | Bussiere, D.E.,Pratt, S.D.,Katz, L.,Severin, J.M.,Holzman, T.,Park, C.H. The Structure of VanX Reveals a Novel Amino-Dipeptidase Involved in Mediating Transposon-Based Vancomycin Resistance Mol.Cell, 2:75-84, 1998 Cited by PubMed Abstract: VanX is a zinc-dependent D-alanyl-D-alanine dipeptidase that is a critical component in a system that mediates transposon-based vancomycin resistance in enterococci. It is also a key drug target in circumventing clinical vancomycin resistance. The structure of VanX from E. faecium has been solved by X-ray crystallography and reveals a Zn(2+)-dipeptidase with a unique overall fold and a well-defined active site confined within a cavity of limited size. The crystal structures of VanX, the VanX:D-alanyl-D-alanine complex, the VanX:D-alanine complex, and VanX in complex with phosphonate and phosphinate transition-state analog inhibitors, are also presented at high resolution. Structural homology searches of known structures revealed that the fold of VanX is similar to those of two proteins: the N-terminal fragment of murine Sonic hedgehog and the Zn(2+)-dependent N-acyl-D-alanyl-D-alanine carboxypeptidase of S. albus G. PubMed: 9702193DOI: 10.1016/S1097-2765(00)80115-X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
Download full validation report
