2jbv

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[[Image:2jbv.jpg|left|200px]]
[[Image:2jbv.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 2jbv |SIZE=350|CAPTION= <scene name='initialview01'>2jbv</scene>, resolution 1.86&Aring;
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The line below this paragraph, containing "STRUCTURE_2jbv", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Fao+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Dms+Binding+Site+For+Chain+A'>AC2</scene>, <scene name='pdbsite=AC3:Fao+Binding+Site+For+Chain+B'>AC3</scene>, <scene name='pdbsite=AC4:Dms+Binding+Site+For+Chain+B'>AC4</scene>, <scene name='pdbsite=AC5:Unx+Binding+Site+For+Chain+A'>AC5</scene>, <scene name='pdbsite=AC6:Unx+Binding+Site+For+Chain+A'>AC6</scene>, <scene name='pdbsite=AC7:Unx+Binding+Site+For+Chain+B'>AC7</scene> and <scene name='pdbsite=AC8:Unx+Binding+Site+For+Chain+B'>AC8</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=FAO:[(2R,3S,4R,5R)-5-(6-AMINO-9H-PURIN-9-YL)-3,4-DIHYDROXYTETRAHYDROFURAN-2-YL]METHYL+(2R,3S,4S)-5-[(4AS,10AR)-7,8-DIMETHYL-2,4-DIOXO-1,3,4,4A,5,10A-HEXAHYDROBENZO[G]PTERIDIN-10(2H)-YL]-2,3,4-TRIHYDROXYPENTYL+DIHYDROGEN+DIPHOSPHATE'>FAO</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Choline_oxidase Choline oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.17 1.1.3.17] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_2jbv| PDB=2jbv | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jbv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jbv OCA], [http://www.ebi.ac.uk/pdbsum/2jbv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2jbv RCSB]</span>
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}}
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'''CRYSTAL STRUCTURE OF CHOLINE OXIDASE REVEALS INSIGHTS INTO THE CATALYTIC MECHANISM'''
'''CRYSTAL STRUCTURE OF CHOLINE OXIDASE REVEALS INSIGHTS INTO THE CATALYTIC MECHANISM'''
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[[Category: Lountos, G T.]]
[[Category: Lountos, G T.]]
[[Category: Orville, A M.]]
[[Category: Orville, A M.]]
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[[Category: alcohol oxidation]]
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[[Category: Alcohol oxidation]]
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[[Category: arthrobacter globiformi]]
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[[Category: Arthrobacter globiformi]]
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[[Category: c4a-adduct]]
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[[Category: C4a-adduct]]
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[[Category: covalently linked fad]]
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[[Category: Covalently linked fad]]
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[[Category: flavoenyzme oxidase]]
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[[Category: Flavoenyzme oxidase]]
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[[Category: flavoprotein]]
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[[Category: Flavoprotein]]
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[[Category: glucose-methanol-choline oxidoreductase enzyme superfamily]]
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[[Category: Glucose-methanol-choline oxidoreductase enzyme superfamily]]
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[[Category: oxidoreductase]]
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[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 08:39:48 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:55:54 2008''
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Revision as of 05:39, 4 May 2008

Image:2jbv.jpg

Template:STRUCTURE 2jbv

CRYSTAL STRUCTURE OF CHOLINE OXIDASE REVEALS INSIGHTS INTO THE CATALYTIC MECHANISM


Overview

Choline oxidase catalyzes the oxidation of choline to glycine betaine, a compatible solute that accumulates in pathogenic bacteria and plants so they can withstand osmotic and temperature stresses. The crystal structure of choline oxidase was determined and refined to a resolution of 1.86 A with data collected at 100 K using synchrotron X-ray radiation. The structure reveals a covalent linkage between His99 Nepsilon2 and FAD C8M atoms, and a 123 A3 solvent-excluded cavity adjacent to the re face of the flavin. A hypothetical model for choline docked into the cavity suggests that several aromatic residues and Glu312 may orient the cationic substrate for efficient catalysis. The role of the negative charge on Glu312 was investigated by engineering variant enzymes in which Glu312 was replaced with alanine, glutamine, or aspartate. The Glu312Ala enzyme was inactive. The Glu312Gln enzyme exhibited a Kd value for choline at least 500 times larger than that of the wild-type enzyme. The Glu312Asp enzyme had a kcat/KO2 value similar to that of the wild-type enzyme but kcat and kcat/Km values that were 230 and 35 times lower, respectively, than in the wild-type enzyme. These data are consistent with the spatial location of the negative charge on residue 312 being important for the oxidation of the alcohol substrate. Solvent viscosity and substrate kinetic isotope effects suggest the presence of an internal equilibrium in the Glu312Asp enzyme prior to the hydride transfer reaction. Altogether, the crystallographic and mechanistic data suggest that Glu312 is important for binding and positioning of the substrate in the active site of choline oxidase.

About this Structure

2JBV is a Single protein structure of sequence from Arthrobacter globiformis. Full crystallographic information is available from OCA.

Reference

Role of Glu312 in binding and positioning of the substrate for the hydride transfer reaction in choline oxidase., Quaye O, Lountos GT, Fan F, Orville AM, Gadda G, Biochemistry. 2008 Jan 8;47(1):243-56. Epub 2007 Dec 12. PMID:18072756 Page seeded by OCA on Sun May 4 08:39:48 2008

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