PDBsum entry 5df8

Transferase

PDB id: 5df8

Contents

Protein chains

514 a.a.

489 a.a.

Ligands

59F ×2

GOL ×6

Metals

_CL ×6

Waters ×598

PDB id:

5df8

Name:

Transferase

Title:

Crystal structure of penicillin-binding protein 3 from pseudomonas aeruginosa in complex with cefoperazone

Structure:

Cell division protein. Chain: a, b. Synonym: penicillin-binding protein 3,pseudomonas aeruginosa genome assembly pae221. Engineered: yes

Source:

Pseudomonas aeruginosa. Organism_taxid: 287. Gene: pbpb, ftsi_2, ers445055_04698, pae221_03076, yq19_27590. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008

Resolution:

2.00Å R-factor: 0.228 R-free: 0.263

Authors:

J.Ren,J.E.Nettleship,A.Males,D.I.Stuart,R.J.Owens

Key ref:

J.Ren et al. (2016). Crystal structures of penicillin-binding protein 3 in complexes with azlocillin and cefoperazone in both acylated and deacylated forms. Febs Lett, 590, 288-297. PubMed id: 26823174 DOI: 10.1002/1873-3468.12054

Date:

26-Aug-15 Release date: 13-Jan-16

Protein chain

Q51504  (Q51504_PSEAI) -  Peptidoglycan D,D-transpeptidase FtsI from Pseudomonas aeruginosa

Seq: 579 a.a.

Struc: 514 a.a.

Protein chain

Q51504  (Q51504_PSEAI) -  Peptidoglycan D,D-transpeptidase FtsI from Pseudomonas aeruginosa

Seq: 579 a.a.

Struc: 489 a.a.

Enzyme reactions

• Enzyme class: Chains A, B: E.C.3.4.16.4 - serine-type D-Ala-D-Ala carboxypeptidase.
• Reaction: D-alanyl-D-alanine + H₂O = 2 D-alanine

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

DOI no: 10.1002/1873-3468.12054

Febs Lett 590:288-297 (2016)

PubMed id: 26823174

Crystal structures of penicillin-binding protein 3 in complexes with azlocillin and cefoperazone in both acylated and deacylated forms.

J.Ren, J.E.Nettleship, A.Males, D.I.Stuart, R.J.Owens.

ABSTRACT

Penicillin-binding protein 3 (PBP3) from Pseudomonas aeruginosa is the molecular target of β-lactam-based antibiotics. Structures of PBP3 in complexes with azlocillin and cefoperazone, which are in clinical use for the treatment of pseudomonad infections, have been determined to 2.0 Å resolution. Together with data from other complexes, these structures identify a common set of residues involved in the binding of β-lactams to PBP3. Comparison of wild-type and an active site mutant (S294A) showed that increased thermal stability of PBP3 following azlocillin binding was entirely due to covalent binding to S294, whereas cefoperazone binding produces some increase in stability without the covalent link. Consistent with this, a third crystal structure was determined in which the hydrolysis product of cefoperazone was noncovalently bound in the active site of PBP3. This is the first structure of a complex between a penicillin-binding protein and cephalosporic acid and may be important in the design of new noncovalent PBP3 inhibitors.