2oov

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:2oov.gif|left|200px]]
[[Image:2oov.gif|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 2oov |SIZE=350|CAPTION= <scene name='initialview01'>2oov</scene>, resolution 1.700&Aring;
+
The line below this paragraph, containing "STRUCTURE_2oov", creates the "Structure Box" on the page.
-
|SITE=
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SME:METHIONINE+SULFOXIDE'>SME</scene>, <scene name='pdbligand=TPQ:5-(2-CARBOXY-2-AMINOETHYL)-2-HYDROXY-1,4-BENZOQUINONE'>TPQ</scene>
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Amine_oxidase_(copper-containing) Amine oxidase (copper-containing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.6 1.4.3.6] </span>
+
or leave the SCENE parameter empty for the default display.
-
|GENE= AMO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4905 Pichia angusta])
+
-->
-
|DOMAIN=
+
{{STRUCTURE_2oov| PDB=2oov | SCENE= }}
-
|RELATEDENTRY=[[1a2v|1A2V]], [[2oqe|2OQE]]
+
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2oov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oov OCA], [http://www.ebi.ac.uk/pdbsum/2oov PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2oov RCSB]</span>
+
-
}}
+
'''Crystal Structure of Hansenula polymorpha amine oxidase to 1.7 Angstroms'''
'''Crystal Structure of Hansenula polymorpha amine oxidase to 1.7 Angstroms'''
Line 23: Line 20:
==Reference==
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/17409383 17409383]
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:[http://www.ncbi.nlm.nih.gov/pubmed/17409383 17409383]
-
[[Category: Amine oxidase (copper-containing)]]
 
[[Category: Pichia angusta]]
[[Category: Pichia angusta]]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Johnson, B J.]]
[[Category: Johnson, B J.]]
[[Category: Wilmot, C M.]]
[[Category: Wilmot, C M.]]
-
[[Category: beta-sandwich]]
+
[[Category: Beta-sandwich]]
-
[[Category: protein-derived cofactor]]
+
[[Category: Protein-derived cofactor]]
-
[[Category: tpq]]
+
[[Category: Tpq]]
-
 
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 11:21:06 2008''
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:20:55 2008''
+

Revision as of 08:21, 4 May 2008

Image:2oov.gif

Template:STRUCTURE 2oov

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.

About this Structure

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

Reference

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 Sun May 4 11:21:06 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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