PDBsum entry 2v3y

Hydrolase

PDB id: 2v3y

Contents

Protein chain

440 a.a. *

Ligands

PRO-LEU

Metals

_CL

_MN ×2

Waters ×732

* Residue conservation analysis

PDB id:

2v3y

Name:

Hydrolase

Title:

His361ala escherichia coli aminopeptidase p in complex with product

Structure:

Xaa-pro aminopeptidase. Chain: a. Synonym: x-pro aminopeptidase, aminopeptidase p ii, app-ii, aminoacylproline aminopeptidase, aminopeptidase p. Engineered: yes. Mutation: yes. Tripeptide (valine-proline-leucine). Chain: b. Engineered: yes.

Source:

Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Organism_taxid: 562

Resolution:

1.60Å R-factor: 0.154 R-free: 0.167

Authors:

S.C.Graham,J.M.Guss

Key ref:

S.C.Graham and J.M.Guss (2008). Complexes of mutants of Escherichia coli aminopeptidase P and the tripeptide substrate ValProLeu. Arch Biochem Biophys, 469, 200-208. PubMed id: 17983589

Date:

25-Jun-07 Release date: 20-Nov-07

Protein chain

P15034  (AMPP_ECOLI) -  Xaa-Pro aminopeptidase from Escherichia coli (strain K12)

Seq: 441 a.a.

Struc: 440 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.3.4.11.9 - Xaa-Pro aminopeptidase.
• Reaction: Release of any N-terminal amino acid, including proline, that is linked with proline, even from a dipeptide or tripeptide.
• Cofactor: Cobalt cation or Mn(2+)

Arch Biochem Biophys 469:200-208 (2008)

PubMed id: 17983589

Complexes of mutants of Escherichia coli aminopeptidase P and the tripeptide substrate ValProLeu.

S.C.Graham, J.M.Guss.

ABSTRACT

Aminopeptidase P (APPro) is a manganese-containing enzyme that catalyses the hydrolysis of the N-terminal residue of a polypeptide if the second residue is proline. Structures of APPro mutants with reduced or negligible activity have been determined in complex with the tripeptide substrate ValProLeu. In the complex of Glu383Ala APPro with ValProLeu one of the two metal sites is only partly occupied, indicating an essential role for Glu383 in metal binding in the presence of substrate. His361Ala APPro clearly possesses residual activity as the ValProLeu substrate has been cleaved in the crystals; difference electron density consistent with bound ProLeu dipeptide and a disordered Val amino acid is present at the active site. Contrary to previous suggestions, the His243Ala mutant is capable of binding substrate. The structure of the His243Ala APPro complex with ValProLeu shows that the peptide interacts with one of the active-site metal atoms via its terminal amino group. The implications of these complexes for the roles of the respective residues in APPro catalysis are discussed.