PDBsum entry 2prq

Hydrolase

PDB id: 2prq

Contents

Protein chain

291 a.a. *

Ligands

TRS

Metals

_CO ×2

Waters ×76

* Residue conservation analysis

PDB id:

2prq

Name:

Hydrolase

Title:

X-ray crystallographic characterization of the co(ii)-substituted tris-bound form of the aminopeptidase from aeromonas proteolytica

Structure:

Bacterial leucyl aminopeptidase. Chain: a. Fragment: residues 107-397. Engineered: yes

Source:

Vibrio proteolyticus. Organism_taxid: 671. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.15Å R-factor: 0.224 R-free: 0.273

Authors:

P.Munih,A.Moulin,C.C.Stamper,B.Bennet,D.Ringe,G.A.Petsko,R.C.Holz

Key ref:

P.Munih et al. (2007). X-ray crystallographic characterization of the Co(II)-substituted Tris-bound form of the aminopeptidase from Aeromonas proteolytica. J Inorg Biochem, 101, 1099-1107. PubMed id: 17574677

Date:

04-May-07 Release date: 12-Jun-07

Protein chain

Q01693  (AMPX_VIBPR) -  Bacterial leucyl aminopeptidase from Vibrio proteolyticus

Seq: 504 a.a.

Struc: 291 a.a.

Enzyme reactions

• Enzyme class: E.C.3.4.11.10 - bacterial leucyl aminopeptidase.
• Reaction: Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
• Cofactor: Zn(2+)

J Inorg Biochem 101:1099-1107 (2007)

PubMed id: 17574677

X-ray crystallographic characterization of the Co(II)-substituted Tris-bound form of the aminopeptidase from Aeromonas proteolytica.

P.Munih, A.Moulin, C.C.Stamper, B.Bennett, D.Ringe, G.A.Petsko, R.C.Holz.

ABSTRACT

The X-ray crystal structure of the Co(II)-loaded form of the aminopeptidase from Aeromonas proteolytica ([CoCo(AAP)]) was solved to 2.2A resolution. [CoCo(AAP)] folds into an alpha/beta globular domain with a twisted beta-sheet hydrophobic core sandwiched between alpha-helices, identical to [ZnZn(AAP)]. Co(II) binding to AAP does not introduce any major conformational changes to the overall protein structure and the amino acid residues ligated to the dicobalt(II) cluster in [CoCo(AAP)] are the same as those in the native Zn(II)-loaded structure with only minor perturbations in bond lengths. The Co(II)-Co(II) distance is 3.3A. Tris(hydroxymethyl)aminomethane (Tris) coordinates to the dinuclear Co(II) active site of AAP with one of the Tris hydroxyl oxygen atoms (O4) forming a single oxygen atom bridge between the two Co(II) ions. This is the only Tris atom coordinated to the metals with Co1-O and Co2-O bonds distances of 2.2 and 1.9A, respectively. Each of the Co(II) ions resides in a distorted trigonal bipyramidal geometry. This important structure bridges the gap between previous structural and spectroscopic studies performed on AAP and is discussed in this context.