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[[Image:1n4w.gif|left|200px]]


{{Structure
==ATOMIC RESOLUTION STRUCTURE OF CHOLESTEROL OXIDASE @ pH 7.3 (STREPTOMYCES SP. SA-COO)==
|PDB= 1n4w |SIZE=350|CAPTION= <scene name='initialview01'>1n4w</scene>, resolution 0.92&Aring;
<StructureSection load='1n4w' size='340' side='right'caption='[[1n4w]], [[Resolution|resolution]] 0.92&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>
<table><tr><td colspan='2'>[[1n4w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._SA-COO Streptomyces sp. SA-COO]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N4W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N4W FirstGlance]. <br>
|ACTIVITY= <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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.92&#8491;</td></tr>
|GENE= CHOA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1931 Streptomyces sp.])
<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>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1n4w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n4w OCA], [https://pdbe.org/1n4w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n4w RCSB], [https://www.ebi.ac.uk/pdbsum/1n4w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n4w ProSAT]</span></td></tr>
|RELATEDENTRY=[[1b4v|1B4V]], [[1b8s|1B8S]], [[1cbo|1CBO]], [[1cc2|1CC2]], [[1ijh|1IJH]], [[1n1p|1N1P]], [[1n4v|1N4V]], [[1n4u|1N4U]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n4w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n4w OCA], [http://www.ebi.ac.uk/pdbsum/1n4w PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1n4w RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/CHOD_STRS0 CHOD_STRS0] Bifunctional enzyme that catalyzes the oxidation of the 3-beta-hydroxy group of cholesterol and the isomerization of the double bond of the resulting product.
== 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/n4/1n4w_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=1n4w ConSurf].
<div style="clear:both"></div>


'''ATOMIC RESOLUTION STRUCTURE OF CHOLESTEROL OXIDASE @ pH 7.3 (STREPTOMYCES SP. SA-COO)'''
==See Also==
 
*[[Cholesterol oxidase|Cholesterol oxidase]]
 
__TOC__
==Overview==
</StructureSection>
Hydrogen atoms are a vital component of enzyme structure and function. In recent years, atomic resolution crystallography (&gt;or=1.2 A) has been successfully used to investigate the role of the hydrogen atom in enzymatic catalysis. Here, atomic resolution crystallography was used to study the effect of pH on cholesterol oxidase from Streptomyces sp., a flavoenzyme oxidoreductase. Crystallographic observations of the anionic oxidized flavin cofactor at basic pH are consistent with the UV-visible absorption profile of the enzyme and readily explain the reversible pH-dependent loss of oxidation activity. Furthermore, a hydrogen atom, positioned at an unusually short distance from the main chain carbonyl oxygen of Met122 at high pH, was observed, suggesting a previously unknown mechanism of cofactor stabilization. This study shows how a redox active site responds to changes in the enzyme's environment and how these changes are able to influence the mechanism of enzymatic catalysis.
[[Category: Large Structures]]
 
[[Category: Streptomyces sp. SA-COO]]
==About this Structure==
[[Category: Lario PI]]
1N4W is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_sp. Streptomyces sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N4W OCA].
[[Category: Vrielink A]]
 
==Reference==
Atomic resolution crystallography reveals how changes in pH shape the protein microenvironment., Lyubimov AY, Lario PI, Moustafa I, Vrielink A, Nat Chem Biol. 2006 May;2(5):259-64. Epub 2006 Apr 9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16604066 16604066]
[[Category: Cholesterol oxidase]]
[[Category: Single protein]]
[[Category: Streptomyces sp.]]
[[Category: Lario, P I.]]
[[Category: Vrielink, A.]]
[[Category: atomic resolution]]
[[Category: flavoenzyme]]
[[Category: oxidoreductase]]
[[Category: steroid metabolism]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:25:31 2008''

Latest revision as of 10:52, 14 February 2024

ATOMIC RESOLUTION STRUCTURE OF CHOLESTEROL OXIDASE @ pH 7.3 (STREPTOMYCES SP. SA-COO)ATOMIC RESOLUTION STRUCTURE OF CHOLESTEROL OXIDASE @ pH 7.3 (STREPTOMYCES SP. SA-COO)

Structural highlights

1n4w is a 1 chain structure with sequence from Streptomyces sp. SA-COO. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 0.92Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CHOD_STRS0 Bifunctional enzyme that catalyzes the oxidation of the 3-beta-hydroxy group of cholesterol and the isomerization of the double bond of the resulting product.

Evolutionary Conservation

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

See Also

1n4w, resolution 0.92Å

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