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3cox

From Proteopedia

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[[Image:3cox.gif|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF CHOLESTEROL OXIDASE COMPLEXED WITH A STEROID SUBSTRATE. IMPLICATIONS FOR FAD DEPENDENT ALCOHOL OXIDASES==
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|PDB= 3cox |SIZE=350|CAPTION= <scene name='initialview01'>3cox</scene>, resolution 1.8&Aring;
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<StructureSection load='3cox' size='340' side='right'caption='[[3cox]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene>
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<table><tr><td colspan='2'>[[3cox]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Brevibacterium_sterolicum Brevibacterium sterolicum]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1cox 1cox]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3COX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3COX FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Cholesterol_oxidase Cholesterol oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.6 1.1.3.6]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3cox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cox OCA], [https://pdbe.org/3cox PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cox RCSB], [https://www.ebi.ac.uk/pdbsum/3cox PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cox ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CHOD_BREST CHOD_BREST] Catalyzes the oxidation and isomerization of cholesterol to cholestenone (4-cholesten-3-one), which is an initial step in the cholesterol degradation process.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/co/3cox_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3cox ConSurf].
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<div style="clear:both"></div>
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'''CRYSTAL STRUCTURE OF CHOLESTEROL OXIDASE COMPLEXED WITH A STEROID SUBSTRATE. IMPLICATIONS FOR FAD DEPENDENT ALCOHOL OXIDASES'''
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==See Also==
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*[[Cholesterol oxidase|Cholesterol oxidase]]
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__TOC__
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==Overview==
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</StructureSection>
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Cholesterol oxidase from Brevibacterium sterolicum is a flavin-dependent enzyme that catalyzes the oxidation and isomerization of 3 beta-hydroxy steroids with a double bond at delta 5-delta 6 of the steroid ring backbone. The crystal structure of the free enzyme in the absence of a steroid substrate has previously been determined. In this paper we report the crystal structure of the complex of cholesterol oxidase with the steroid substrate dehydroisoandrosterone, refined at 1.8-A resolution. The final crystallographic R-value is 15.7% for all reflections between 10.0- and 1.8-A resolution. The steroid is buried within the protein in an internal cavity which, in the free enzyme crystal structure, was occupied by a lattice of water molecules. The conformations of a number of side chains lining the active-site cavity have changed in order to accommodate the steroid substrate. A loop region of the structure between residues 70 and 90 differs significantly between the substrate-free and substrate-bound forms of the enzyme, presumably to facilitate binding of the steroid. The hydroxyl group of the steroid substrate is hydrogen-bonded to both the flavin ring system of the FAD cofactor and a bound water molecule. FAD-dependent cholesterol oxidase shares significant structural homology with another flavoenzyme, glucose oxidase, suggesting that it might also be a member of the glucose-methanol-choline (GMC) oxidoreductase family. Although there is only limited sequence homology, a superposition of these two structures reveals a conserved histidine residue within hydrogen-bonding distance of the active-site water molecule.(ABSTRACT TRUNCATED AT 250 WORDS)
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==About this Structure==
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3COX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Brevibacterium_sterolicum Brevibacterium sterolicum]. This structure supersedes the now removed PDB entry 1COX. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3COX OCA].
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==Reference==
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Crystal structure of cholesterol oxidase complexed with a steroid substrate: implications for flavin adenine dinucleotide dependent alcohol oxidases., Li J, Vrielink A, Brick P, Blow DM, Biochemistry. 1993 Nov 2;32(43):11507-15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8218217 8218217]
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[[Category: Brevibacterium sterolicum]]
[[Category: Brevibacterium sterolicum]]
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[[Category: Cholesterol oxidase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Blow DM]]
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[[Category: Blow, D M.]]
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[[Category: Brick P]]
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[[Category: Brick, P.]]
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[[Category: Li J]]
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[[Category: Li, J.]]
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[[Category: Vrielink A]]
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[[Category: Vrielink, A.]]
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[[Category: FAD]]
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[[Category: oxidoreductase(oxygen receptor)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:04:10 2008''
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Current revision

CRYSTAL STRUCTURE OF CHOLESTEROL OXIDASE COMPLEXED WITH A STEROID SUBSTRATE. IMPLICATIONS FOR FAD DEPENDENT ALCOHOL OXIDASES

PDB ID 3cox

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