4WBG

Crystal structure of class C beta-lactamase Mox-1 covalently complexed with aztorenam

Summary for 4WBG

• Entry DOI: 10.2210/pdb4wbg/pdb
• Related: 3W8K
• Descriptor: Beta-lactamase, 2-({[(1Z)-1-(2-amino-1,3-thiazol-4-yl)-2-oxo-2-{[(2S,3S)-1-oxo-3-(sulfoamino)butan-2-yl]amino}ethylidene]amino}oxy)-2-methylpropanoic acid, ZINC ION, ... (5 entities in total)
• Functional Keywords: beta-lactamase, aztreonam, acyl-intermediate, hydrolase
• Biological source: Klebsiella pneumoniae
• Total number of polymer chains: 1
• Total formula weight: 41662.39

Authors

Oguri, T.,Shimizu-ibuka, A.,Ishii, Y. (deposition date: 2014-09-03, release date: 2015-07-01, Last modification date: 2024-10-23)

Primary citation

Oguri, T.,Ishii, Y.,Shimizu-Ibuka, A.
Conformational Change Observed in the Active Site of Class C beta-Lactamase MOX-1 upon Binding to Aztreonam
Antimicrob.Agents Chemother., 59:5069-5072, 2015

PubMed Abstract: We solved the crystal structure of the class C β-lactamase MOX-1 complexed with the inhibitor aztreonam at 1.9Å resolution. The main-chain oxygen of Ser315 interacts with the amide nitrogen of aztreonam. Surprisingly, compared to that in the structure of free MOX-1, this main-chain carboxyl changes its position significantly upon binding to aztreonam. This result indicates that the interaction between MOX-1 and β-lactams can be accompanied by conformational changes in the B3 β-strand main chain.

PubMed: 26055361
DOI: 10.1128/AAC.04428-14

Experimental method

X-RAY DIFFRACTION (1.9 Å)