PDBsum entry 2ctb

HydrolasE(C-terminal peptidase)

PDB id: 2ctb

Contents

Protein chain

307 a.a. *

Metals

_ZN

Waters ×218

* Residue conservation analysis

PDB id:

2ctb

Name:

HydrolasE(C-terminal peptidase)

Title:

The high resolution crystal structure of the complex between carboxypeptidase a and l-phenyl lactate

Structure:

Carboxypeptidase a. Chain: a. Engineered: yes

Source:

Bos taurus. Cattle. Organism_taxid: 9913

Resolution:

1.50Å R-factor: 0.100

Authors:

A.Teplyakov,K.S.Wilson,P.Orioli,S.Mangani

Key ref:

A.Teplyakov et al. (1993). High-resolution structure of the complex between carboxypeptidase A and L-phenyl lactate. Acta Crystallogr D Biol Crystallogr, 49, 534-540. PubMed id: 15299490 DOI: 10.1107/S0907444993007267

Date:

02-Apr-93 Release date: 31-Jan-94

Protein chain

P00730  (CBPA1_BOVIN) -  Carboxypeptidase A1 from Bos taurus

Seq: 419 a.a.

Struc: 307 a.a.

Enzyme reactions

• Enzyme class: E.C.3.4.17.1 - carboxypeptidase A.
• Reaction: Peptidyl-L-amino acid + H₂O = peptide + L-amino acid
• Cofactor: Zn(2+)

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

Added reference

DOI no: 10.1107/S0907444993007267

Acta Crystallogr D Biol Crystallogr 49:534-540 (1993)

PubMed id: 15299490

High-resolution structure of the complex between carboxypeptidase A and L-phenyl lactate.

A.Teplyakov, K.S.Wilson, P.Orioli, S.Mangani.

ABSTRACT

The X-ray structures of native carboxypeptidase A and of the enzyme-inhibitor complex with L-phenyl lactate have been refined at 1.54 and 1.45 A resolution to R factors of 0.151 and 0.161, respectively. Crystals of the complex were isomorphous with the native crystals (space group P2(1), a = 51.60, b = 60.27, c = 47.25 A, beta = 97.27 degrees ). The high-resolution electron density allowed correction of many side-chain positions in the classical carboxypeptidase A model. This reflects the advantages of the high-quality complete synchrotron data collected with an imaging plate detector. The conformational changes in the active centre of the enzyme upon binding of the inhibitor are restricted to only two residues, Tyr248 and Arg145. L-Phenyl lactate is bound in the S1' pocket and forms hydrogen bonds to Arg145, Glu270 and to the zinc-bound water molecule. The present structure provides an explanation for the higher stability of the complexes with the products of esterolysis in comparison with those of amidolysis. This is consistent with the finding that product release is rate limiting for esters but not for peptides.

Selected figure(s)

Figure 2.
Fig. 2. The ~o/~ plot for the native CPA model.

Figure 3.
Fig. 3. Representaive fragment of the (3Fo­ 2Fc) lectron density of CPA contoured at the level of 1.Str, where o­ is the root­mean­square deviation. The present CPA model is shown in green, the 5CPA odel is shown in orange. (a) Ser254 and Ile255; (b) Leu271 and Tyr238 with the hydrogen­bonded water molecule.

The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (1993, 49, 534-540) copyright 1993.

Figures were selected by an automated process.