1coy: Difference between revisions

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New page: left|200px<br /><applet load="1coy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1coy, resolution 1.8Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1coy.gif|left|200px]]<br /><applet load="1coy" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1coy, resolution 1.8&Aring;" />
'''CRYSTAL STRUCTURE OF CHOLESTEROL OXIDASE COMPLEXED WITH A STEROID SUBSTRATE. IMPLICATIONS FOR FAD DEPENDENT ALCOHOL OXIDASES'''<br />


==Overview==
==CRYSTAL STRUCTURE OF CHOLESTEROL OXIDASE COMPLEXED WITH A STEROID SUBSTRATE. IMPLICATIONS FOR FAD DEPENDENT ALCOHOL OXIDASES==
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)
<StructureSection load='1coy' size='340' side='right'caption='[[1coy]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1coy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Brevibacterium_sterolicum Brevibacterium sterolicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1COY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1COY FirstGlance]. <br>
</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>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AND:3-BETA-HYDROXY-5-ANDROSTEN-17-ONE'>AND</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1coy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1coy OCA], [https://pdbe.org/1coy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1coy RCSB], [https://www.ebi.ac.uk/pdbsum/1coy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1coy ProSAT]</span></td></tr>
</table>
== Function ==
[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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/co/1coy_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1coy ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1COY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Brevibacterium_sterolicum Brevibacterium sterolicum] with AND and FAD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1COY OCA].
*[[Cholesterol oxidase|Cholesterol oxidase]]
 
__TOC__
==Reference==
</StructureSection>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=8218217 8218217]
[[Category: Brevibacterium sterolicum]]
[[Category: Brevibacterium sterolicum]]
[[Category: Cholesterol oxidase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Blow DM]]
[[Category: Blow, D.M.]]
[[Category: Brick P]]
[[Category: Brick, P.]]
[[Category: Li J]]
[[Category: Li, J.]]
[[Category: Vrielink A]]
[[Category: Vrielink, A.]]
[[Category: AND]]
[[Category: FAD]]
[[Category: oxidoreductase(oxygen receptor)]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:38:12 2007''

Latest revision as of 09:44, 7 February 2024

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

Structural highlights

1coy is a 1 chain structure with sequence from Brevibacterium sterolicum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1coy, resolution 1.80Å

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