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.


1ci9

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ci9.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1ci9.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ci9| PDB=1ci9 | SCENE= }}
{{STRUCTURE_1ci9| PDB=1ci9 | SCENE= }}
-
'''DFP-INHIBITED ESTERASE ESTB FROM BURKHOLDERIA GLADIOLI'''
+
===DFP-INHIBITED ESTERASE ESTB FROM BURKHOLDERIA GLADIOLI===
-
==Overview==
+
<!--
-
Esterases form a diverse class of enzymes of largely unknown physiological role. Because many drugs and pesticides carry ester functions, the hydrolysis of such compounds forms at least one potential biological function. Carboxylesterases catalyze the hydrolysis of short chain aliphatic and aromatic carboxylic ester compounds. Esterases, D-alanyl-D-alanine-peptidases (DD-peptidases) and beta-lactamases can be grouped into two distinct classes of hydrolases with different folds and topologically unrelated catalytic residues, the one class comprising of esterases, the other one of beta-lactamases and DD-peptidases. The chemical reactivities of esters and beta-lactams towards hydrolysis are quite similar, which raises the question of which factors prevent esterases from displaying beta-lactamase activity and vice versa. Here we describe the crystal structure of EstB, an esterase isolated from Burkholderia gladioli. It shows the protein to belong to a novel class of esterases with homology to Penicillin binding proteins, notably DD-peptidase and class C beta-lactamases. Site-directed mutagenesis and the crystal structure of the complex with diisopropyl-fluorophosphate suggest Ser75 within the "beta-lactamase" Ser-x-x-Lys motif to act as catalytic nucleophile. Despite its structural homology to beta-lactamases, EstB shows no beta-lactamase activity. Although the nature and arrangement of active-site residues is very similar between EstB and homologous beta-lactamases, there are considerable differences in the shape of the active site tunnel. Modeling studies suggest steric factors to account for the enzyme's selectivity for ester hydrolysis versus beta-lactam cleavage.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11847270}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11847270 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11847270}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Caboxylesterase]]
[[Category: Caboxylesterase]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:45:34 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:46:49 2008''

Revision as of 17:46, 30 June 2008

Image:1ci9.png

Template:STRUCTURE 1ci9

DFP-INHIBITED ESTERASE ESTB FROM BURKHOLDERIA GLADIOLI

Template:ABSTRACT PUBMED 11847270

About this Structure

1CI9 is a Single protein structure of sequence from Burkholderia gladioli. Full crystallographic information is available from OCA.

Reference

EstB from Burkholderia gladioli: a novel esterase with a beta-lactamase fold reveals steric factors to discriminate between esterolytic and beta-lactam cleaving activity., Wagner UG, Petersen EI, Schwab H, Kratky C, Protein Sci. 2002 Mar;11(3):467-78. PMID:11847270

Page seeded by OCA on Mon Jun 30 20:46:49 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ci9"
Personal tools