PDBsum entry: 1jji

Hydrolase

PDB id: 1jji

Contents

Protein chains

311 a.a. *

Ligands

EPE ×4

Waters ×561

* Residue conservation analysis

PDB id:

1jji

Name:

Hydrolase

Title:

The crystal structure of a hyper-thermophilic carboxylestera the archaeon archaeoglobus fulgidus

Structure:

Carboxylesterase. Chain: a, b, c, d. Engineered: yes

Source:

Archaeoglobus fulgidus. Organism_taxid: 2234. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

2.20Å R-factor: 0.203 R-free: 0.235

Authors:

G.De Simone,V.Menchise,G.Manco,L.Mandrich,N.Sorrentino,D.Lan M.Rossi,C.Pedone

Key ref:

G.De Simone et al. (2001). The crystal structure of a hyper-thermophilic carboxylesterase from the archaeon Archaeoglobus fulgidus. J Mol Biol, 314, 507-518. PubMed id: 11846563 DOI: 10.1006/jmbi.2001.5152

Date:

06-Jul-01 Release date: 05-Dec-01

Protein chains

O28558  (O28558_ARCFU) -  Carboxylesterase (EstA)

Seq: 311 a.a.

Struc: 311 a.a.

 Gene Ontology (GO) functional annotation 

• Biological process: metabolic process (1 term)
• Biochemical function: hydrolase activity (1 term)

DOI no: 10.1006/jmbi.2001.5152

J Mol Biol 314:507-518 (2001)

PubMed id: 11846563

The crystal structure of a hyper-thermophilic carboxylesterase from the archaeon Archaeoglobus fulgidus.

G.De Simone, V.Menchise, G.Manco, L.Mandrich, N.Sorrentino, D.Lang, M.Rossi, C.Pedone.

ABSTRACT

The crystal structure of AFEST, a novel hyper-thermophilic carboxylesterase from the archaeon Archaeoglobus fulgidus, complexed with a sulphonyl derivative, has been determined and refined to 2.2 A resolution. This enzyme, which has recently been classified as a member of the hormone- sensitive-lipase (H) group of the esterase/lipase superfamily, presents a canonical alpha/beta hydrolase core, shielded on the C-terminal side by a cap region composed of five alpha-helices. It contains the catalytic triad Ser160, His285 and Asp255, whereby the nucleophile is covalently modified and the oxyanion hole formed by Gly88, Gly89 and Ala161. A structural comparison of AFEST with its mesophilic and thermophilic homologues, Brefeldin A esterase from Bacillus subtilis (BFAE) and EST2 from Alicyclobacillus acidocaldarius, reveals an increase in the number of intramolecular ion pairs and secondary structure content, as well as a significant reduction in loop extensions and ratio of hydrophobic to charged surface area. The variety of structural differences suggests possible strategies for thermostabilization of lipases and esterases with potential industrial applications.

Selected figure(s)

Figure 1.
Figure 1. Overall fold of AFEST: b-strands and helices belonging to the canonical a/b hydrolase fold are shown in yellow and in red, respectively, while helices forming the cap domain are shown in blue. The residues of the catalytic triad are shown in ball-and-stick representation: Ser160 bound to the Hepes molecule (cyan), His285 (magenta) and Asp255 (green). Generated using Molscript[67].

Figure 3.
Figure 3. The AFEST dimer viewed normal to the molecular 2-fold axis. Subunit A is shown in red and subunit B in green. The active site residues are shown as ball-and-stick. This Figure was generated with the program Molscript[67].

The above figures are reprinted by permission from Elsevier: J Mol Biol (2001, 314, 507-518) copyright 2001.

Figures were selected by an automated process.