PDBsum entry 2gzb

Hydrolase inhibitor

PDB id: 2gzb

Contents

Protein chains

164 a.a. *

Metals

IOD ×10

Waters ×245

* Residue conservation analysis

PDB id:

2gzb

Name:

Hydrolase inhibitor

Title:

Bauhinia bauhinioides cruzipain inhibitor (bbci)

Structure:

Kunitz-type proteinase inhibitor bbci. Chain: a, b. Engineered: yes

Source:

Bauhinia bauhinioides. Organism_taxid: 166014. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.70Å R-factor: 0.201 R-free: 0.244

Authors:

D.Hansen,S.Macedo-Ribeiro,M.V.A.S.Navarro,R.C.Garratt,M.L.V.Oliva

Key ref:

D.Hansen et al. (2007). Crystal structure of a novel cysteinless plant Kunitz-type protease inhibitor. Biochem Biophys Res Commun, 360, 735-740. PubMed id: 17631863

Date:

11-May-06 Release date: 17-Jul-07

Protein chains

P83051  (BBCI_BAUBA) -  Kunitz-type proteinase inhibitor BbCI from Bauhinia bauhinioides

Seq: 164 a.a.

Struc: 164 a.a.

Enzyme reactions

• Enzyme class: E.C.?

Biochem Biophys Res Commun 360:735-740 (2007)

PubMed id: 17631863

Crystal structure of a novel cysteinless plant Kunitz-type protease inhibitor.

D.Hansen, S.Macedo-Ribeiro, P.Veríssimo, S.Yoo Im, M.U.Sampaio, M.L.Oliva.

ABSTRACT

Bauhinia bauhinioides Cruzipain Inhibitor (BbCI) is a cysteine protease inhibitor highly homologous to plant Kunitz-type inhibitors. However, in contrast to classical Kunitz family inhibitors it lacks cysteine residues and therefore disulfide bridges. BbCI is also distinct in the ability to inactivate enzymes belonging to two different classes, cysteine and serine proteases. Besides inhibiting the cysteine protease cruzipain, BbCI also inhibits cathepsin L and the serine proteases HNE (human neutrophil elastase) and PPE (porcine pancreatic elastase). Monoclinic crystals of the recombinant inhibitor that diffract to 1.7A resolution were obtained using hanging drop method by vapor diffusion at 18 degrees C. The refined structure shows the conservative beta-trefoil fold features of the Kunitz inhibitors. In BbCI, one of the two characteristic S-S bonds is replaced by the water-mediated interaction between Tyr125 and Gly132. In this work we explore the structural differences between Kunitz-type inhibitors and analyze the essential interactions that maintain the protein structural stability preserving its biological function.