1vm1
From Proteopedia
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| , resolution 2.02Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , and | ||||||
| Gene: | BLA (Klebsiella pneumoniae) | ||||||
| Activity: | Beta-lactamase, with EC number 3.5.2.6 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF SHV-1 BETA-LACTAMASE INHIBITED BY TAZOBACTAM
Overview
Two species resulting from the reaction of the SHV-1 class A beta-lactamase with the sulfone inhibitor tazobactam have been trapped at 100 K and mapped by X-ray crystallography at 2.0 A resolution. An acyclic form of tazobactam is covalently bonded to the catalytic Ser70 side chain, and a second species, a five-atom vinyl carboxylic acid fragment of tazobactam, is bonded to Ser130. It is proposed that the electron density map of the crystal is a composite picture of two complexes, each with only a single bound species. It is estimated that the two complexes exist in the crystal in approximately equal populations. Results are discussed in relation to the mechanism-based inhibition of class A beta-lactamases by the similar inhibitors sulbactam and clavulanic acid.
About this Structure
1VM1 is a Single protein structure of sequence from Klebsiella pneumoniae. This structure supersedes the now removed PDB entry 1G56. Full crystallographic information is available from OCA.
Reference
Inhibition of the SHV-1 beta-lactamase by sulfones: crystallographic observation of two reaction intermediates with tazobactam., Kuzin AP, Nukaga M, Nukaga Y, Hujer A, Bonomo RA, Knox JR, Biochemistry. 2001 Feb 13;40(6):1861-6. PMID:11327849
Page seeded by OCA on Thu Mar 20 14:47:20 2008
Categories: Beta-lactamase | Klebsiella pneumoniae | Single protein | Bonomo, R A. | Hujer, A. | Knox, J R. | Kuzin, A P. | Nukaga, M. | Nukaga, Y. | AKR | MA4 | TAZ | TBE | Beta-lactam hydrolase | Detergent binding | Inhibitor design | Penicillinase
