2vcy

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px <!-- The line below this paragraph, containing "STRUCTURE_2vcy", creates the "Structure Box" on the page. You may change the PDB parameter (which sets the PD...)
Line 1: Line 1:
-
[[Image:2vcy.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2vcy.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2vcy| PDB=2vcy | SCENE= }}
{{STRUCTURE_2vcy| PDB=2vcy | SCENE= }}
-
'''CRYSTAL STRUCTURE OF 2-ENOYL THIOESTER REDUCTASE OF HUMAN FAS II'''
+
===CRYSTAL STRUCTURE OF 2-ENOYL THIOESTER REDUCTASE OF HUMAN FAS II===
-
==Overview==
+
<!--
-
Structural and kinetic properties of the human 2-enoyl thioester reductase [mitochondrial enoyl-coenzyme A reductase (MECR)/ETR1] of the mitochondrial fatty acid synthesis (FAS) II pathway have been determined. The crystal structure of this dimeric enzyme (at 2.4 A resolution) suggests that the binding site for the recognition helix of the acyl carrier protein is in a groove between the two adjacent monomers. This groove is connected via the pantetheine binding cleft to the active site. The modeled mode of NADPH binding, using molecular dynamics calculations, suggests that Tyr94 and Trp311 are critical for catalysis, which is supported by enzyme kinetic data. A deep, water-filled pocket, shaped by hydrophobic and polar residues and extending away from the catalytic site, was recognized. This pocket can accommodate a fatty acyl tail of up to 16 carbons. Mutagenesis of the residues near the end of this pocket confirms the importance of this region for the binding of substrate molecules with long fatty acyl tails. Furthermore, the kinetic analysis of the wild-type MECR/ETR1 shows a bimodal distribution of catalytic efficiencies, in agreement with the notion that two major products are generated by the mitochondrial FAS II pathway.
+
The line below this paragraph, {{ABSTRACT_PUBMED_18479707}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 18479707 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_18479707}}
==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Polymorphism]]
[[Category: Polymorphism]]
[[Category: Transit peptide]]
[[Category: Transit peptide]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 4 09:53:15 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:51:27 2008''

Revision as of 00:51, 29 July 2008

Image:2vcy.png

Template:STRUCTURE 2vcy

CRYSTAL STRUCTURE OF 2-ENOYL THIOESTER REDUCTASE OF HUMAN FAS II

Template:ABSTRACT PUBMED 18479707

About this Structure

2VCY is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural enzymological studies of 2-enoyl thioester reductase of the human mitochondrial FAS II pathway: new insights into its substrate recognition properties., Chen ZJ, Pudas R, Sharma S, Smart OS, Juffer AH, Hiltunen JK, Wierenga RK, Haapalainen AM, J Mol Biol. 2008 Jun 13;379(4):830-44. Epub 2008 Apr 24. PMID:18479707

Page seeded by OCA on Tue Jul 29 03:51:27 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2vcy"
Personal tools