2oov: Difference between revisions

Revision as of 02:41, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2oov.png

Template:STRUCTURE 2oov

Crystal Structure of Hansenula polymorpha amine oxidase to 1.7 AngstromsCrystal Structure of Hansenula polymorpha amine oxidase to 1.7 Angstroms

Template:ABSTRACT PUBMED 17409383

About this StructureAbout this Structure

2OOV is a Protein complex structure of sequences from Pichia angusta. Full crystallographic information is available from OCA.

ReferenceReference

Exploring molecular oxygen pathways in Hansenula polymorpha copper-containing amine oxidase., Johnson BJ, Cohen J, Welford RW, Pearson AR, Schulten K, Klinman JP, Wilmot CM, J Biol Chem. 2007 Jun 15;282(24):17767-76. Epub 2007 Apr 4. PMID:17409383

Page seeded by OCA on Tue Jul 29 02:41:11 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:2oov.gif|left|200px]]
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-'''Crystal Structure of Hansenula polymorpha amine oxidase to 1.7 Angstroms'''
+===Crystal Structure of Hansenula polymorpha amine oxidase to 1.7 Angstroms===
-==Overview==
+<!--
-The accessibility of large substrates to buried enzymatic active sites is dependent upon the utilization of proteinaceous channels. The necessity of these channels in the case of small substrates is questionable because diffusion through the protein matrix is often assumed. Copper amine oxidases contain a buried protein-derived quinone cofactor and a mononuclear copper center that catalyze the conversion of two substrates, primary amines and molecular oxygen, to aldehydes and hydrogen peroxide, respectively. The nature of molecular oxygen migration to the active site in the enzyme from Hansenula polymorpha is explored using a combination of kinetic, x-ray crystallographic, and computational approaches. A crystal structure of H. polymorpha amine oxidase in complex with xenon gas, which serves as an experimental probe for molecular oxygen binding sites, reveals buried regions of the enzyme suitable for transient molecular oxygen occupation. Calculated O(2) free energy maps using copper amine oxidase crystal structures in the absence of xenon correspond well with later experimentally observed xenon sites in these systems, and allow the visualization of O(2) migration routes of differing probabilities within the protein matrix. Site-directed mutagenesis designed to block individual routes has little effect on overall k(cat)/K(m) (O(2)), supporting multiple dynamic pathways for molecular oxygen to reach the active site.
+The line below this paragraph, {{ABSTRACT_PUBMED_17409383}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17409383 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17409383}}
 ==About this Structure==
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 [[Category: Protein-derived cofactor]]
 [[Category: Tpq]]
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