2gew: Difference between revisions

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-{{Seed}}
-[[Image:2gew.png|left|200px]]
-<!--
+==Atomic resolution structure of cholesterol oxidase @ pH 9.0 (Streptomyces sp. SA-COO)==
-The line below this paragraph, containing "STRUCTURE_2gew", creates the "Structure Box" on the page.
+<StructureSection load='2gew' size='340' side='right'caption='[[2gew]], [[Resolution|resolution]] 0.97&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2gew]] 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=2GEW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GEW FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.97&#8491;</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>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-{{STRUCTURE_2gew|  PDB=2gew  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2gew FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gew OCA], [https://pdbe.org/2gew PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gew RCSB], [https://www.ebi.ac.uk/pdbsum/2gew PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gew ProSAT]</span></td></tr>
+</table>
+== 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/ge/2gew_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=2gew ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-===Atomic resolution structure of cholesterol oxidase @ pH 9.0 (Streptomyces sp. SA-COO)===
+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:16604066<ref>PMID:16604066</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2gew" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_16604066}}, adds the Publication Abstract to the page
+*[[Cholesterol oxidase|Cholesterol oxidase]]
-(as it appears on PubMed at http://www.pubmed.gov), where 16604066 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_16604066}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-GEW 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=2GEW OCA].
+[[Category: Streptomyces sp. SA-COO]]
+[[Category: Lyubimov AY]]
-==Reference==
+[[Category: Vrielink A]]
-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: Lyubimov, A Y.]]
-[[Category: Vrielink, A]]
-[[Category: Atomic resolution]]
-[[Category: Flavoenzyme]]
-[[Category: Hydrogen bond]]
-[[Category: Oxidoreductase]]
-[[Category: Steroid metabolism]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:57:15 2008''