This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1evq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1evq.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1evq.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1evq| PDB=1evq | SCENE= }}
{{STRUCTURE_1evq| PDB=1evq | SCENE= }}
-
'''THE CRYSTAL STRUCTURE OF THE THERMOPHILIC CARBOXYLESTERASE EST2 FROM ALICYCLOBACILLUS ACIDOCALDARIUS'''
+
===THE CRYSTAL STRUCTURE OF THE THERMOPHILIC CARBOXYLESTERASE EST2 FROM ALICYCLOBACILLUS ACIDOCALDARIUS===
-
==Overview==
+
<!--
-
EST2 is a novel thermophilic carboxylesterase, isolated and cloned from Alicyclobacillus (formerly Bacillus) acidocaldarius, which optimally hydrolyses esters with acyl chain lengths of six to eight carbon atoms at 70 degrees C. On the basis of the amino acid sequence homology, it has been classified as a member of the mammalian hormone-sensitive lipase (HSL) subfamily.The crystal structure of EST2, complexed with a sulphonyl derivative, has been determined at 2.6 A resolution by a multiple wavelength anomalous diffraction experiment on a seleno-methionine derivative. EST2 presents a canonical alpha/beta hydrolase core, shielded at the C-terminal side by a cap region built up of five helices. It contains the lipase-like catalytic triad, Ser155, His282 and Asp252, whereby the nucleophile is covalently modified. This allows an unambiguous view of the putative active site of EST2, detecting the oxyanion hole, in whose formation the amino acid sequence motif His81-Gly82-Gly83-Gly84 is involved, and the hydrophobic binding pocket for the acyl chain. The structural model here reported provides the first example of a transition state analogue of an esterase/lipase belonging to the HSL group, thus affording useful information for the design of medical inhibitors. Moreover, as the first X-ray structure of a thermophilic carboxylesterase, the comparison with its mesophilic homologue, the Brefeldin A esterase (BFAE) from Bacillus subtilis, allows the identification of putative determinants of thermal stability.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11061974}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11061974 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11061974}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Simone, G De.]]
[[Category: Simone, G De.]]
[[Category: Alpha/beta hydrolase fold]]
[[Category: Alpha/beta hydrolase fold]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:34:29 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:05:44 2008''

Revision as of 23:05, 30 June 2008

Image:1evq.png

Template:STRUCTURE 1evq

THE CRYSTAL STRUCTURE OF THE THERMOPHILIC CARBOXYLESTERASE EST2 FROM ALICYCLOBACILLUS ACIDOCALDARIUS

Template:ABSTRACT PUBMED 11061974

About this Structure

1EVQ is a Single protein structure of sequence from Alicyclobacillus acidocaldarius. Full crystallographic information is available from OCA.

Reference

A snapshot of a transition state analogue of a novel thermophilic esterase belonging to the subfamily of mammalian hormone-sensitive lipase., De Simone G, Galdiero S, Manco G, Lang D, Rossi M, Pedone C, J Mol Biol. 2000 Nov 10;303(5):761-71. PMID:11061974

Page seeded by OCA on Tue Jul 1 02:05:44 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1evq"
Personal tools