3bf8

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:3bf8.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:3bf8.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_3bf8| PDB=3bf8 | SCENE= }}
{{STRUCTURE_3bf8| PDB=3bf8 | SCENE= }}
-
'''1.1 resolution structure of ybfF, a new esterase from Escherichia coli: a unique substrate-binding crevice generated by domain arrangement'''
+
===1.1 resolution structure of ybfF, a new esterase from Escherichia coli: a unique substrate-binding crevice generated by domain arrangement===
-
==Overview==
+
<!--
-
Esterases are one of the most common enzymes and are involved in diverse cellular functions. ybfF protein from Escherichia coli (Ec_ybfF) belongs to the esterase family for the large substrates, palmitoyl coenzyme A and malonyl coenzyme A, which are important cellular intermediates for energy conversion and biomolecular synthesis. To obtain molecular information on ybfF esterase, which is found in a wide range of microorganisms, we elucidated the crystal structures of Ec_ybfF in complexes with small molecules at resolutions of 1.1 and 1.68 A, respectively. The structure of Ec_ybfF is composed of a globular alpha/beta hydrolase domain with a three-helical bundle cap, which is linked by a kinked helix to the alpha/beta hydrolase domain. It contains a catalytic tetrad of Ser-His-Asp-Ser with the first Ser acting as a nucleophile. The unique spatial arrangement and orientation of the helical cap with respect to the alpha/beta hydrolase domain form a substrate-binding crevice for large substrates. The helical cap is also directly involved in catalysis by providing a substrate anchor, viz., the conserved residues of Arg123 and Tyr208. The high-resolution structure of Ec_ybfF shows that the inserted helical bundle structure and its spatial orientation with respect to the alpha/beta hydrolase domain are critical for creating a large inner space and constituting a specific active site, thereby providing the broad substrate spectrum toward large biomolecules.
+
The line below this paragraph, {{ABSTRACT_PUBMED_18215690}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 18215690 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_18215690}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Thioesterase]]
[[Category: Thioesterase]]
[[Category: Ybff]]
[[Category: Ybff]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:42:42 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:23:47 2008''

Revision as of 16:23, 27 July 2008

Template:STRUCTURE 3bf8

1.1 resolution structure of ybfF, a new esterase from Escherichia coli: a unique substrate-binding crevice generated by domain arrangement

Template:ABSTRACT PUBMED 18215690

About this Structure

3BF8 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

High-resolution structure of ybfF from Escherichia coli K12: a unique substrate-binding crevice generated by domain arrangement., Park SY, Lee SH, Lee J, Nishi K, Kim YS, Jung CH, Kim JS, J Mol Biol. 2008 Mar 7;376(5):1426-37. Epub 2008 Jan 4. PMID:18215690

Page seeded by OCA on Sun Jul 27 19:23:47 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools