1HSK

CRYSTAL STRUCTURE OF S. AUREUS MURB

Summary for 1HSK

• Entry DOI: 10.2210/pdb1hsk/pdb
• Descriptor: UDP-N-ACETYLENOLPYRUVOYLGLUCOSAMINE REDUCTASE, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• Functional Keywords: peptidoglycan synthesis, cell wall, cell division, oxidoreductase, nadp, flavoprotein, fad
• Biological source: Staphylococcus aureus
• Cellular location: Cytoplasm (By similarity): P61431
• Total number of polymer chains: 1
• Total formula weight: 36804.28

Authors

Benson, T.E.,Harris, M.S.,Choi, G.H.,Cialdella, J.I.,Herberg, J.T.,Martin Jr., J.P.,Baldwin, E.T. (deposition date: 2000-12-27, release date: 2001-03-14, Last modification date: 2024-02-07)

Primary citation

Benson, T.E.,Harris, M.S.,Choi, G.H.,Cialdella, J.I.,Herberg, J.T.,Martin Jr., J.P.,Baldwin, E.T.
A structural variation for MurB: X-ray crystal structure of Staphylococcus aureus UDP-N-acetylenolpyruvylglucosamine reductase (MurB).
Biochemistry, 40:2340-2350, 2001

PubMed Abstract: The X-ray crystal structure of the substrate free form of Staphylococcus aureus UDP-N-acetylenolpyruvylglucosamine reductase (MurB) has been solved to 2.3 A resolution with an R-factor of 20.3% and a free R-factor of 22.3%. While the overall fold of the S. aureus enzyme is similar to that of the homologous Escherichia coli MurB X-ray crystal structure, notable distinctions between the S. aureus and E. coli MurB protein structures occur in residues involved in substrate binding. Analysis of available MurB sequences from other bacteria suggest that the S. aureus MurB structure is representative of a distinct structural class of UDP-N-acetylenolpyruvylglucosamine reductases including Bacillus subtilis and Helicobacter pylori that are characterized by a modified mechanism for substrate binding.

PubMed: 11327854
DOI: 10.1021/bi002162d

Experimental method

X-RAY DIFFRACTION (2.3 Å)