1LL5

X-ray crystal structure of AmpC WT beta-lactamase in complex with covalently bound imipenem

Summary for 1LL5

• Entry DOI: 10.2210/pdb1ll5/pdb
• Related: 1BT5 1FCO 1KE4
• Descriptor: beta-lactamase, (5R)-5-[(1S,2R)-1-formyl-2-hydroxypropyl]-3-[(2-{[(E)-iminomethyl]amino}ethyl)sulfanyl]-4,5-dihydro-1H-pyrrole-2-carbox ylic acid (3 entities in total)
• Functional Keywords: beta-lactamase, carbapenem, imipenem, hydrolase
• Biological source: Escherichia coli
• Cellular location: Periplasm: P00811
• Total number of polymer chains: 2
• Total formula weight: 79778.57

Authors

Beadle, B.M.,Shoichet, B.K. (deposition date: 2002-04-26, release date: 2002-11-27, Last modification date: 2023-08-16)

Primary citation

Beadle, B.M.,Shoichet, B.K.
Structural Basis for Imipenem Inhibition of Class C beta-lactamases
ANTIMICROB.AGENTS CHEMOTHER., 46:3978-3980, 2002

PubMed Abstract: To determine how imipenem inhibits the class C beta-lactamase AmpC, the X-ray crystal structure of the acyl-enzyme complex was determined to a resolution of 1.80 A. In the complex, the lactam carbonyl oxygen of imipenem has flipped by approximately 180 degrees compared to its expected position; the electrophilic acyl center is thus displaced from the point of hydrolytic attack. This conformation resembles that of imipenem bound to the class A enzyme TEM-1 but is different from that of moxalactam bound to AmpC.

PubMed: 12435704
DOI: 10.1128/AAC.46.12.3978-3980.2002

Experimental method

X-RAY DIFFRACTION (1.8 Å)