PDBsum entry 2de9

Hydrolase

PDB id: 2de9

Contents

Protein chain

240 a.a. *

Ligands

SO4 ×2

Waters ×292

* Residue conservation analysis

PDB id:

2de9

Name:

Hydrolase

Title:

Crystal structure of porcine pancreatic elastase complexed with tris after soaking a tris-free solution

Structure:

Elastase-1. Chain: a. Ec: 3.4.21.36

Source:

Sus scrofa. Pig. Organism_taxid: 9823. Tissue: pancreas

Resolution:

1.30Å R-factor: 0.211 R-free: 0.226

Authors:

T.Kinoshita,T.Tada

Key ref:

T.Kinoshita et al. (2006). Tris(hydroxymethyl)aminomethane induces conformational change and crystal-packing contraction of porcine pancreatic elastase. Acta Crystallogr Sect F Struct Biol Cryst Commun, 62, 623-626. PubMed id: 16820677 DOI: 10.1107/S1744309106023001

Date:

09-Feb-06 Release date: 11-Jul-06

Protein chain

P00772  (CELA1_PIG) -  Chymotrypsin-like elastase family member 1 from Sus scrofa

Seq: 266 a.a.

Struc: 240 a.a.

Enzyme reactions

• Enzyme class: E.C.3.4.21.36 - pancreatic elastase.
• Reaction: Hydrolysis of proteins, including elastin. Preferential cleavage: Ala-|-Xaa.

DOI no: 10.1107/S1744309106023001

Acta Crystallogr Sect F Struct Biol Cryst Commun 62:623-626 (2006)

PubMed id: 16820677

Tris(hydroxymethyl)aminomethane induces conformational change and crystal-packing contraction of porcine pancreatic elastase.

T.Kinoshita, A.Yamaguchi, T.Tada.

ABSTRACT

Porcine pancreatic elastase (PPE) was crystallized under new sulfate-free conditions containing 0.3 M NaCl and 50 mM tris(hydroxymethyl)aminomethane-HCl at pH 7.0. The crystal structure determined at 1.5 angstroms resolution had a unique conformation in four regions which contained loop portions. A chloride ion was bound near the catalytic triad instead of the sulfate ion in PDB entry 1qnj, a typical PPE crystal structure. However, the chloride ion did not affect the configuration of the catalytic triad. A tris(hydroxymethyl)aminomethane (Tris) molecule was bound to the S4 and S5 subsites in place of the adjacent molecule in the 1qnj crystal and played a significant role in the structural change of the region. The distortion in this region may subsequently have induced conformational changes in the other three regions. The fact that Tris and these four regions make a diagonal line in the ac plane may have affected the crystal-packing contraction along the a and c axes in the crystal compared with the typical crystal.

Selected figure(s)

Figure 1.
C^[alpha] traces of the NaCl/Tris form (blue) and the 1qnj structure (orange). The catalytic triad, Ser195, His57 and Asp102, is shown in a ball-and-stick representation. A chloride ion (green ball) binds near the catalytic triad and Tris (displayed in stick representation) binds to the S4 and S5 subsites. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 July 1; 62(Pt 7): 623–626. Published online 2006 June 26. doi: 10.1107/S1744309106023001. Copyright [copyright] International Union of Crystallography 2006

Figure 3.
Configurations of the catalytic triad in the NaCl/Tris form and the 1qnj form (magenta). Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 July 1; 62(Pt 7): 623–626. Published online 2006 June 26. doi: 10.1107/S1744309106023001. Copyright [copyright] International Union of Crystallography 2006

The above figures are reprinted from an Open Access publication published by the IUCr: Acta Crystallogr Sect F Struct Biol Cryst Commun (2006, 62, 623-626) copyright 2006.

Figures were selected by an automated process.