1UXY

MURB MUTANT WITH SER 229 REPLACED BY ALA, COMPLEX WITH ENOLPYRUVYL-UDP-N-ACETYLGLUCOSAMINE

Summary for 1UXY

• Entry DOI: 10.2210/pdb1uxy/pdb
• Descriptor: URIDINE DIPHOSPHO-N-ACETYLENOLPYRUVYLGLUCOSAMINE REDUCTASE, FLAVIN-ADENINE DINUCLEOTIDE, URIDINE-DIPHOSPHATE-2(N-ACETYLGLUCOSAMINYL) BUTYRIC ACID, ... (4 entities in total)
• Functional Keywords: peptidoglycan synthesis, cell wall, cell division, oxidoreductase, nadp, flavoprotein, fad
• Biological source: Escherichia coli
• Cellular location: Cytoplasm (Probable): P08373
• Total number of polymer chains: 1
• Total formula weight: 39093.56

Authors

Benson, T.E.,Walsh, C.T.,Hogle, J.M. (deposition date: 1996-11-08, release date: 1997-04-01, Last modification date: 2024-02-14)

Primary citation

Benson, T.E.,Walsh, C.T.,Hogle, J.M.
X-ray crystal structures of the S229A mutant and wild-type MurB in the presence of the substrate enolpyruvyl-UDP-N-acetylglucosamine at 1.8-A resolution.
Biochemistry, 36:806-811, 1997

PubMed Abstract: MurB catalyzes the second committed step in the synthesis of peptidoglycan, a key component of the bacterial cell wall. The crystal structures of both a S229A mutant and wild-type MurB in the presence of the substrate enolpyruvyl-UDP-N-acetylglucosamine were solved and refined at 1.8 A resolution. The single point mutation of residue 229 from serine to alanine eliminated a hydroxyl group which has previously been proposed to play a critical role as a proton donor during the second half-reaction of MurB, namely, reoxidation of FADH2 and reduction of the enolpyruvyl substrate. The mutation also resulted in the loss of the water molecule-hydrogen bonded to the serine hydroxyl in the wild-type structure changing the hydrogen-bonding network with in the active site. Comparison of the wild-type and S229A mutant structures confirms that the dramatic kinetic defect of an approximately 10(7)-fold decrease observed for the Ser 229 Ala mutant in the second half-reaction [Benson, T.E., Walsh, C.T., & Massey, V. (1997) Biochemistry 36, 796-805] is a direct result of the loss of the serine hydroxyl moiety rather than other nonspecific active-site changes or general structural defects.

PubMed: 9020778
DOI: 10.1021/bi962221g

Experimental method

X-RAY DIFFRACTION (1.8 Å)