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.


2f5v

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2f5v.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2f5v.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2f5v| PDB=2f5v | SCENE= }}
{{STRUCTURE_2f5v| PDB=2f5v | SCENE= }}
-
'''Reaction geometry and thermostability mutant of pyranose 2-oxidase from the white-rot fungus Peniophora sp.'''
+
===Reaction geometry and thermostability mutant of pyranose 2-oxidase from the white-rot fungus Peniophora sp.===
-
==Overview==
+
<!--
-
Pyranose 2-oxidase catalyzes the oxidation of a number of carbohydrates using dioxygen; glucose, for example, is oxidized at carbon 2. The structure of pyranose 2-oxidase with the reaction product 2-keto-beta-d-glucose bound in the active center is reported in a new crystal form at 1.41 A resolution. The binding structure suggests that the alpha-anomer cannot be processed. The binding mode of the oxidized product was used to model other sugars accepted by the enzyme and to explain its specificity and catalytic rates. The reported structure at pH 6.0 shows a drastic conformational change in the loop of residues 454-461 (loop 454-461) at the active center compared to that of a closely homologous enzyme analyzed at pH 4.5 with a bound acetate inhibitor. In our structures, the loop is highly mobile and shifts to make way for the sugar to pass into the active center. Presumably, loop 454-461 functions as a gatekeeper. Apart from the wild-type enzyme, a thermostable variant was analyzed at 1.84 A resolution. In this variant, Glu542 is exchanged for a lysine. The observed stabilization could be a result of the mutated residue changing an ionic contact at a comparatively weak interface of the tetramer.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16716069}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16716069 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16716069}}
==About this Structure==
==About this Structure==
Line 35: Line 39:
[[Category: Rossmann-fold]]
[[Category: Rossmann-fold]]
[[Category: Tetramer]]
[[Category: Tetramer]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:29:44 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:21:37 2008''

Revision as of 13:21, 28 July 2008

Image:2f5v.png

Template:STRUCTURE 2f5v

Reaction geometry and thermostability mutant of pyranose 2-oxidase from the white-rot fungus Peniophora sp.

Template:ABSTRACT PUBMED 16716069

About this Structure

2F5V is a Single protein structure of sequence from Peniophora sp. sg. Full crystallographic information is available from OCA.

Reference

Reaction geometry and thermostable variant of pyranose 2-oxidase from the white-rot fungus Peniophora sp., Bannwarth M, Heckmann-Pohl D, Bastian S, Giffhorn F, Schulz GE, Biochemistry. 2006 May 30;45(21):6587-95. PMID:16716069

Page seeded by OCA on Mon Jul 28 16:21:37 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2f5v"
Personal tools