1i19: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(One intermediate revision by the same user not shown)
Line 3: Line 3:
<StructureSection load='1i19' size='340' side='right'caption='[[1i19]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='1i19' size='340' side='right'caption='[[1i19]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1i19]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/'brevibacterium_sterolicum' 'brevibacterium sterolicum']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I19 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1I19 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1i19]] is a 2 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=1I19 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I19 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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]] 1.7&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1i19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i19 OCA], [http://pdbe.org/1i19 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1i19 RCSB], [http://www.ebi.ac.uk/pdbsum/1i19 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1i19 ProSAT]</span></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=1i19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i19 OCA], [https://pdbe.org/1i19 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i19 RCSB], [https://www.ebi.ac.uk/pdbsum/1i19 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i19 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q7SID9_BREST Q7SID9_BREST]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 18: Line 20:
</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=1i19 ConSurf].
</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=1i19 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cholesterol oxidase is a monomeric flavoenzyme that catalyzes the oxidation and isomerization of cholesterol to cholest-4-en-3-one. Two forms of the enzyme are known, one containing the cofactor non-covalently bound to the protein and one in which the cofactor is covalently linked to a histidine residue. The x-ray structure of the enzyme from Brevibacterium sterolicum containing covalently bound FAD has been determined and refined to 1.7-A resolution. The active site consists of a cavity sealed off from the exterior of the protein. A model for the steroid substrate, cholesterol, can be positioned in the pocket revealing the structural factors that result in different substrate binding affinities between the two known forms of the enzyme. The structure suggests that Glu(475), located at the active site cavity, may act as the base for both the oxidation and the isomerization steps of the catalytic reaction. A water-filled channel extending toward the flavin moiety, inside the substrate-binding cavity, may act as the entry point for molecular oxygen for the oxidative half-reaction. An arginine and a glutamate residue at the active site, found in two conformations are proposed to control oxygen access to the cavity from the channel. These concerted side chain movements provide an explanation for the biphasic mode of reaction with dioxygen and the ping-pong kinetic mechanism exhibited by the enzyme.
Oxygen access to the active site of cholesterol oxidase through a narrow channel is gated by an Arg-Glu pair.,Coulombe R, Yue KQ, Ghisla S, Vrielink A J Biol Chem. 2001 Aug 10;276(32):30435-41. Epub 2001 Jun 7. PMID:11397813<ref>PMID:11397813</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1i19" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Cholesterol oxidase|Cholesterol oxidase]]
*[[Cholesterol oxidase|Cholesterol oxidase]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Brevibacterium sterolicum]]
[[Category: Brevibacterium sterolicum]]
[[Category: Cholesterol oxidase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Coulombe, R]]
[[Category: Coulombe R]]
[[Category: Ghisla, S]]
[[Category: Ghisla S]]
[[Category: Vrielink, A]]
[[Category: Vrielink A]]
[[Category: Yue, K Q]]
[[Category: Yue KQ]]
[[Category: Covalent fad]]
[[Category: Flavoenzyme]]
[[Category: Mix alpha beta]]
[[Category: Oxidoreductase]]

Latest revision as of 10:43, 3 April 2024

CRYSTAL STRUCTURE OF CHOLESTEROL OXIDASE FROM B.STEROLICUMCRYSTAL STRUCTURE OF CHOLESTEROL OXIDASE FROM B.STEROLICUM

Structural highlights

1i19 is a 2 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 1.7Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q7SID9_BREST

Evolutionary Conservation

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

See Also

1i19, resolution 1.70Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=1i19&oldid=4120424"