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.


4eng

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:4eng.gif|left|200px]]
+
{{Seed}}
 +
[[Image:4eng.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_4eng| PDB=4eng | SCENE= }}
{{STRUCTURE_4eng| PDB=4eng | SCENE= }}
-
'''STRUCTURE OF ENDOGLUCANASE V CELLOHEXAOSE COMPLEX'''
+
===STRUCTURE OF ENDOGLUCANASE V CELLOHEXAOSE COMPLEX===
-
==Overview==
+
<!--
-
The structure of the catalytic core of the endoglucanase V (EGV) from Humicola insolens has been determined by the method of multiple isomorphous replacement at 1.5 A resolution. The final model, refined with X-PLOR and PROLSQ, has a crystallographic R factor of 0.163 (R(free) = 0.240) with deviations from stereochemical target values of 0.012 A and 0.037 degrees for bonds and angles, respectively. The model was further refined with SHELXL, including anisotropic modelling of the protein-atom temperature factors, to give a final model with an R factor of 0.105 and an R(free) of 0.154. The initial isomorphous replacement electron-density map was poor and uninterpretable but was improved by the use of synchrotron data collected at a wavelength chosen so as to optimize the f" contribution of the anomalous scattering from the heavy atoms. The structure of H. insolens EGV consists of a six-stranded beta-barrel domain, similar to that found in a family of plant defence proteins, linked by a number of disulfide-bonded loop regions. A long open groove runs across the surface of the enzyme either side of which lie the catalytic aspartate residues. The 9 A separation of the catalytic carboxylate groups is consistent with the observation that EGV catalyzes the hydrolysis of the cellulose, beta(1--&gt;4) links with inversion of configuration at the anomeric C1 atom. This structure is the first representative from the glycosyl hydrolase family 45.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15299721}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15299721 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15299721}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Glycosyl hydrolase]]
[[Category: Glycosyl hydrolase]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:23:16 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 13:35:31 2008''

Revision as of 10:35, 3 July 2008

Template:STRUCTURE 4eng

STRUCTURE OF ENDOGLUCANASE V CELLOHEXAOSE COMPLEX

Template:ABSTRACT PUBMED 15299721

About this Structure

4ENG is a Single protein structure of sequence from Humicola insolens. Full crystallographic information is available from OCA.

Reference

Structure determination and refinement of the Humicola insolens endoglucanase V at 1.5 A resolution., Davies GJ, Dodson G, Moore MH, Tolley SP, Dauter Z, Wilson KS, Rasmussen G, Schulein M, Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):7-17. PMID:15299721

Page seeded by OCA on Thu Jul 3 13:35:31 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools