3M2K

Crystal Structure of fluorescein-labeled Class A -beta lactamase PenP in complex with cefotaxime

Summary for 3M2K

• Entry DOI: 10.2210/pdb3m2k/pdb
• Related: 3LY3 3LY4 3M2J
• Descriptor: Beta-lactamase, CEFOTAXIME, C3' cleaved, open, bound form (3 entities in total)
• Functional Keywords: beta-lactamase, fluorophore, biosensor, hydrolase, cefotaxime, antibiotic resistance, cell membrane, lipoprotein, membrane, palmitate
• Biological source: Bacillus licheniformis
• Total number of polymer chains: 2
• Total formula weight: 57983.55

Authors

Zhao, Y.X.,Leung, Y.C.,Wong, W.T. (deposition date: 2010-03-07, release date: 2011-03-16, Last modification date: 2024-10-09)

Primary citation

Wong, W.T.,Au, H.W.,Yap, H.K.,Leung, Y.C.,Wong, K.Y.,Zhao, Y.
Structural studies of the mechanism for biosensing antibiotics in a fluorescein-labeled beta-lactamase.
BMC Struct. Biol., 11:15-15, 2011

PubMed Abstract: β-lactamase conjugated with environment-sensitive fluorescein molecule to residue 166 on the Ω-loop near its catalytic site is a highly effective biosensor for β-lactam antibiotics. Yet the molecular mechanism of such fluorescence-based biosensing is not well understood.

PubMed: 21443768
DOI: 10.1186/1472-6807-11-15

Experimental method

X-RAY DIFFRACTION (3.5 Å)