3cox: Difference between revisions

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 <StructureSection load='3cox' size='340' side='right'caption='[[3cox]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<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>
+<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>
-</td></tr><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>
+</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cholesterol_oxidase Cholesterol oxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.6 1.1.3.6] </span></td></tr>
+<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>
 <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>
 </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.
+[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]]
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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].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-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)
-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:8218217<ref>PMID:8218217</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3cox" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Cholesterol oxidase|Cholesterol oxidase]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Brevibacterium sterolicum]]
-[[Category: Cholesterol oxidase]]
 [[Category: Large Structures]]
-[[Category: Blow, D M]]
+[[Category: Blow DM]]
-[[Category: Brick, P]]
+[[Category: Brick P]]
-[[Category: Li, J]]
+[[Category: Li J]]
-[[Category: Vrielink, A]]
+[[Category: Vrielink A]]