P.J.Stogios,Z.Wawrzak,G.Minasov,E.Evdokimova,O.Egorova,J.Cosme,R.Di Leo,M.Krishnamoorthy,D.Meziane-Cherif,P.Courvalin,A.Savchenko,W.F.Anderson,Center For Structural Genomics Of Infectious Diseases (Csgid)
Vancomycin antibiotic resistance in Enterococci is mediated by at enzymes of at least six different operons. These enzymes collaborate to alter the normal peptidoglycan layer by converting D-ala-D-ala cross-links into D-ala-D-lac or D-ala-D-ser. These converted peptidoglycan layers are resistant to recognition by vancomycin.
In this entry, we present the structure of VanTg, a serine racemase that converts L-serine to D-serine, which is then incorporated into the vancomycin-resistant cell wall. The structure is dimeric, with each chain comprised of a TIM barrel domain and a primarily-beta sheet containing domain. This structure will be studied to understand the mechanism of L-serine recognition.