spacer
spacer
Go to PDB code: 
protein ligands links
Hydrolase PDB id
1s6r
Jmol
Contents
Protein chain
359 a.a. *
Ligands
IAP
Waters ×47
* Residue conservation analysis
PDB id:
1s6r
Name: Hydrolase
Title: 908r class c beta-lactamase bound to iodo-acetamido-phenyl boronic acid
Structure: Beta-lactamase. Chain: a. Synonym: cephalosporinase. Engineered: yes
Source: Enterobacter cloacae. Organism_taxid: 550. Strain: 908r. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
2.24Å     R-factor:   0.226     R-free:   0.293
Authors: J.Wouters
Key ref: J.Wouters et al. (2003). Crystal structure of Enterobacter cloacae 908R class C beta-lactamase bound to iodo-acetamido-phenyl boronic acid, a transition-state analogue. Cell Mol Life Sci, 60, 1764-1773. PubMed id: 14521155 DOI: 10.1007/s00018-003-3189-2
Date:
27-Jan-04     Release date:   24-Feb-04    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q93CA2  (Q93CA2_ENTCL) -  Beta-lactamase AmpC (Precursor)
Seq:
Struc: 		381 a.a.
359 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.3.5.2.6  - Beta-lactamase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway: 		Penicillin Biosynthesis and Metabolism
      Reaction: A beta-lactam + H2O = a substituted beta-amino acid
      Cofactor: Zinc
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     outer membrane-bounded periplasmic space   1 term 
  Biological process     antibiotic catabolic process   1 term 
  Biochemical function     hydrolase activity     2 terms  

 

 
DOI no: 10.1007/s00018-003-3189-2 Cell Mol Life Sci 60:1764-1773 (2003)
PubMed id: 14521155  
 
 
Crystal structure of Enterobacter cloacae 908R class C beta-lactamase bound to iodo-acetamido-phenyl boronic acid, a transition-state analogue.
J.Wouters, E.Fonzé, M.Vermeire, J.M.Frère, P.Charlier.
 
  ABSTRACT  
 
The structures of the class C beta-lactamase from Enterobacter cloacae 908R alone and in complex with a boronic acid transition-state analogue were determined by X-ray crystallography at 2.1 and 2.3 A, respectively. The structure of the enzyme resembles those of other class C beta-lactamases. The structure of the complex with the transition-state analogue, iodo-acetamido-phenyl boronic acid, shows that the inhibitor is covalently bound to the active-site serine (Ser64). Binding of the inhibitor within the active site is compared with previously determined structures of complexes with other class C enzymes. The structure of the boronic acid adduct indicates ways to improve the affinity of this class of inhibitors. This structure of 908R class C beta-lactamase in complex with a transition-state analogue provides further insights into the mechanism of action of these hydrolases.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20394454 C.Bebrone, P.Lassaux, L.Vercheval, J.S.Sohier, A.Jehaes, E.Sauvage, and M.Galleni (2010).
Current challenges in antimicrobial chemotherapy: focus on ß-lactamase inhibition.
  Drugs, 70, 651-679.  
16677302 J.Y.Kim, H.I.Jung, Y.J.An, J.H.Lee, S.J.Kim, S.H.Jeong, K.J.Lee, P.G.Suh, H.S.Lee, S.H.Lee, and S.S.Cha (2006).
Structural basis for the extended substrate spectrum of CMY-10, a plasmid-encoded class C beta-lactamase.
  Mol Microbiol, 60, 907-916.
PDB code: 1zkj
17077507 M.Hata, Y.Fujii, Y.Tanaka, H.Ishikawa, M.Ishii, S.Neya, M.Tsuda, and T.Hoshino (2006).
Substrate deacylation mechanisms of serine-beta-lactamases.
  Biol Pharm Bull, 29, 2151-2159.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.