› 2adv

X-ray diffraction
2.24Å resolution

Crystal Structures Of Glutaryl 7-Aminocephalosporanic Acid Acylase: mutational study of activation mechanism

Released:
DOI: 10.2210/pdb2adv/pdb
PDB entry 2adv coloured by chain, front view.
PDB entry 2adv coloured by chain, side view.
PDB entry 2adv coloured by chain, top view.
Source organism: Pseudomonas sp. GK16
Primary publication:
Insight into autoproteolytic activation from the structure of cephalosporin acylase: a protein with two proteolytic chemistries.
Kim JK, Yang IS, Shin HJ, Cho KJ, Ryu EK, Kim SH, Park SS, Kim KH
Proc Natl Acad Sci U S A 103 1732-7 (2006)
PMID: 16446446

Function and Biology Details

Reaction catalysed: 
(7R)-7-(4-carboxybutanamido)cephalosporanate + H(2)O = (7R)-7-aminocephalosporanate + glutarate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139684 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Glutaryl-7-aminocephalosporanic-acid acylase subunit alpha Chain: A
Molecule details ›
Chain: A
Length: 166 amino acids
Theoretical weight: 18.21 KDa
Source organism: Pseudomonas sp. GK16
Expression system: Escherichia coli
UniProt:
  • Canonical: P07662 (Residues: 30-195; Coverage: 24%)
Structure domains: Penicillin Amidohydrolase, domain 1
Glutaryl-7-aminocephalosporanic-acid acylase subunit beta Chain: B
Molecule details ›
Chain: B
Length: 28 amino acids
Theoretical weight: 2.95 KDa
Source organism: Pseudomonas sp. GK16
Expression system: Escherichia coli
UniProt:
  • Canonical: P07662 (Residues: 199-226; Coverage: 4%)
Glutaryl-7-aminocephalosporanic-acid acylase subunit beta Chain: C
Molecule details ›
Chain: C
Length: 500 amino acids
Theoretical weight: 56.19 KDa
Source organism: Pseudomonas sp. GK16
Expression system: Escherichia coli
UniProt:
  • Canonical: P07662 (Residues: 227-720; Coverage: 72%)
Sequence domains: Penicillin amidase
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 4A
Spacegroup: P41212
Unit cell:
a: 73.775Å b: 73.775Å c: 384.646Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.183 0.21
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Enzymatic modifications of cephalosporins by cephalosporin acylase and other enzymes.
Sonawane VC. (2006)
2 more

2 mentions without citation

Insight into autoproteolytic activation from the structure of cephalosporin acylase: a protein with two proteolytic chemistries.
Kim et al. (2006)
1 more