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.


2axr

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2axr.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2axr.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2axr| PDB=2axr | SCENE= }}
{{STRUCTURE_2axr| PDB=2axr | SCENE= }}
-
'''Crystal structure of glucooligosaccharide oxidase from Acremonium strictum: a novel flavinylation of 6-S-cysteinyl, 8alpha-N1-histidyl FAD'''
+
===Crystal structure of glucooligosaccharide oxidase from Acremonium strictum: a novel flavinylation of 6-S-cysteinyl, 8alpha-N1-histidyl FAD===
-
==Overview==
+
<!--
-
Glucooligosaccharide oxidase from Acremonium strictum has been screened for potential applications in oligosaccharide acid production and alternative carbohydrate detection, because it catalyzes the oxidation of glucose, maltose, lactose, cellobiose and cello- and maltooligosaccharides. We report the crystal structures of the enzyme and of its complex with an inhibitor, 5-amino-5-deoxy- cellobiono-1,5-lactam at 1.55- and 1.98-A resolution, respectively. Unexpectedly, the protein structure demonstrates the first known double attachment flavinylation, 6-S-cysteinyl, 8alpha-N1-histidyl FAD. The FAD cofactor is cross-linked to the enzyme via the C(6) atom and the 8alpha-methyl group of the isoalloxazine ring with Cys(130) and His(70), respectively. This sugar oxidase possesses an open carbohydrate-binding groove, allowing the accommodation of higher oligosaccharides. The complex structure suggests that this enzyme may prefer a beta-d-glucosyl residue at the reducing end with the conserved Tyr(429) acting as a general base to abstract the OH(1) proton in concert with the H(1) hydride transfer to the flavin N(5). Finally, a detailed comparison illustrates the structural conservation as well as the divergence between this protein and its related flavoenzymes.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16154992}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16154992 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16154992}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Alpha+beta]]
[[Category: Alpha+beta]]
[[Category: Covalent flavoenzyme]]
[[Category: Covalent flavoenzyme]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:36:21 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:27:28 2008''

Revision as of 17:27, 28 July 2008

Image:2axr.png

Template:STRUCTURE 2axr

Crystal structure of glucooligosaccharide oxidase from Acremonium strictum: a novel flavinylation of 6-S-cysteinyl, 8alpha-N1-histidyl FAD

Template:ABSTRACT PUBMED 16154992

About this Structure

2AXR is a Single protein structure of sequence from Acremonium strictum. Full crystallographic information is available from OCA.

Reference

Crystal structure of glucooligosaccharide oxidase from Acremonium strictum: a novel flavinylation of 6-S-cysteinyl, 8alpha-N1-histidyl FAD., Huang CH, Lai WL, Lee MH, Chen CJ, Vasella A, Tsai YC, Liaw SH, J Biol Chem. 2005 Nov 18;280(46):38831-8. Epub 2005 Sep 9. PMID:16154992

Page seeded by OCA on Mon Jul 28 20:27:28 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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