Motion in Mura (Udp-N-Acetylglucosamine Enolpyruvyltransferase) [mura]

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Classification [D-h-2]

Structures
1EJD
1A2N [ PartsList ]

References
E Schönbrunn, S Eschenburg, F Krekel, K Luger, N Amrhein (2000). Role of the loop containing residue 115 in the induced-fit mechanism of the bacterial cell wall biosynthetic enzyme MurA. Biochemistry, 39:2164-73 [Medline info for 10694381]
T Skarzynski, D H Kim, W J Lees, C T Walsh, K Duncan (1998). Stereochemical course of enzymatic enolpyruvyl transfer and catalytic conformation of the active site revealed by the crystal structure of the fluorinated analogue of the reaction tetrahedral intermediate bound to the active site of the C115A mutant of MurA. Biochemistry, 37:2572-7 [Medline info for 9485407]
E Schönbrunn, S Sack, S Eschenburg, A Perrakis, F Krekel, N Amrhein, E Mandelkow (1996). Crystal structure of UDP-N-acetylglucosamine enolpyruvyltransferase, the target of the antibiotic fosfomycin. Structure, 4:1065-75 [Medline info for 8805592]
S Eschenburg, E Schönbrunn (2000). Comparative X-ray analysis of the un-liganded fosfomycin-target murA. Proteins, 40:290-8 [Medline info for 10842342]

GO terms associated with structures
Molecular functiontransferase activity
Biological processUDP-N-acetylgalactosamine biosynthesis

Morphs

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Best representative
Morph Morph name Structure #1 Structure #2 Residues
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Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_ yale.edu