We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1vrx

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1vrx.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1vrx.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1vrx| PDB=1vrx | SCENE= }}
{{STRUCTURE_1vrx| PDB=1vrx | SCENE= }}
-
'''Endocellulase e1 from acidothermus cellulolyticus mutant y245g'''
+
===Endocellulase e1 from acidothermus cellulolyticus mutant y245g===
-
==Overview==
+
<!--
-
&lt;When Tyr245 in endocellulase Cel5A from Acidothermus cellulolyticus was changed to Gly (Y245G) by designed mutation, the value of Ki for inhibition of the enzyme by the product cellobiose was increased more than 1480%. This reduction in product inhibition enabled the mutant enzyme (used in conjunction with Trichoderma reesei cellobiohydrolase-I) to release soluble sugars from biomass cellulose at a rate as much as 40% greater than that achieved by the wild-type (WT) enzyme. The mutant was designed on the basis of the previously published crystal structure of the WT enzyme/substrate complex (at a resolution of 2.4 A), which provided insights into the enzyme mechanism at the atomic level and identified Tyr245 as a key residue interacting with a leaving group. To determine the origin of the change in activity, the crystal structure of Y245G was solved at 2.4-A resolution to an R-factor of 0.19 (R-free = 0.25). To obtain additional information on the enzyme-product interactions, density functional calculations were performed on representative fragments of the WT Cel5A and Y245G. The combined results indicate that the loss of the platform (Y245G) and of a hydrogen bond (from a conformational change in Gln247) reduces the binding energy between product and enzyme by several kilo calories per mole. Both kinetic and structural analyses thus relate the increased enzymatic activity to reduced product inhibition.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15917594}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15917594 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15917594}}
==About this Structure==
==About this Structure==
Line 36: Line 40:
[[Category: Endo-1,4-beta-d-glucanase]]
[[Category: Endo-1,4-beta-d-glucanase]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:51:06 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:05:00 2008''

Revision as of 11:05, 29 July 2008

Image:1vrx.png

Template:STRUCTURE 1vrx

Endocellulase e1 from acidothermus cellulolyticus mutant y245g

Template:ABSTRACT PUBMED 15917594

About this Structure

1VRX is a Single protein structure of sequence from Acidothermus cellulolyticus. This structure supersedes the now removed PDB entry 1c0d. Full crystallographic information is available from OCA.

Reference

Catalytically enhanced endocellulase Cel5A from Acidothermus cellulolyticus., Baker JO, McCarley JR, Lovett R, Yu CH, Adney WS, Rignall TR, Vinzant TB, Decker SR, Sakon J, Himmel ME, Appl Biochem Biotechnol. 2005 Spring;121-124:129-48. PMID:15917594

Page seeded by OCA on Tue Jul 29 14:05:00 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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