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1MBT

OXIDOREDUCTASE

Summary for 1MBT
Entry DOI10.2210/pdb1mbt/pdb
DescriptorURIDINE DIPHOSPHO-N-ACETYLENOLPYRUVYLGLUCOSAMINE REDUCTASE, SULFATE ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (4 entities in total)
Functional Keywordsflavoenzyme, oxidoreductase
Biological sourceEscherichia coli
Cellular locationCytoplasm (Probable): P08373
Total number of polymer chains1
Total formula weight38773.52
Authors
Benson, T.E.,Walsh, C.T.,Hogle, J.M. (deposition date: 1995-11-28, release date: 1996-10-14, Last modification date: 2024-02-14)
Primary citationBenson, T.E.,Walsh, C.T.,Hogle, J.M.
The structure of the substrate-free form of MurB, an essential enzyme for the synthesis of bacterial cell walls.
Structure, 4:47-54, 1996
Cited by
PubMed Abstract: The repeating disaccharide and pentapeptide units of the bacterial peptidoglycan layer are connected by a lactyl ether bridge biosynthesized from UDP-N-acetylglucosamine and phosphoenolpyruvate in sequential enol ether transfer and reduction steps catalyzed by MurA and MurB respectively. Knowledge of the structure and mechanism of the MurB enzyme will permit analysis of this unusual enol ether reduction reaction and may facilitate the design of inhibitors as candidate next-generation antimicrobial agents.
PubMed: 8805513
DOI: 10.1016/S0969-2126(96)00008-1
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

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