2gew: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(11 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:2gew.gif|left|200px]]
<!--
The line below this paragraph, containing "STRUCTURE_2gew", creates the "Structure Box" on the page.
You may change the PDB parameter (which sets the PDB file loaded into the applet)
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
or leave the SCENE parameter empty for the default display.
-->
{{STRUCTURE_2gew|  PDB=2gew  |  SCENE=  }}
'''Atomic resolution structure of cholesterol oxidase @ pH 9.0 (Streptomyces sp. SA-COO)'''


==Atomic resolution structure of cholesterol oxidase @ pH 9.0 (Streptomyces sp. SA-COO)==
<StructureSection load='2gew' size='340' side='right'caption='[[2gew]], [[Resolution|resolution]] 0.97&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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.


==Overview==
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>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2GEW 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].
</div>
<div class="pdbe-citations 2gew" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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]
*[[Cholesterol oxidase|Cholesterol oxidase]]
[[Category: Cholesterol oxidase]]
== References ==
[[Category: Single protein]]
<references/>
[[Category: Streptomyces sp.]]
__TOC__
[[Category: Lyubimov, A Y.]]
</StructureSection>
[[Category: Vrielink, A]]
[[Category: Large Structures]]
[[Category: Atomic resolution]]
[[Category: Streptomyces sp. SA-COO]]
[[Category: Flavoenzyme]]
[[Category: Lyubimov AY]]
[[Category: Hydrogen bond]]
[[Category: Vrielink A]]
[[Category: Oxidoreductase]]
[[Category: Steroid metabolism]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 05:01:25 2008''

Latest revision as of 12:39, 30 August 2023

Atomic resolution structure of cholesterol oxidase @ pH 9.0 (Streptomyces sp. SA-COO)Atomic resolution structure of cholesterol oxidase @ pH 9.0 (Streptomyces sp. SA-COO)

Structural highlights

2gew 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 0.97Å
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.

Publication Abstract from PubMed

Hydrogen atoms are a vital component of enzyme structure and function. In recent years, atomic resolution crystallography (>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 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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Lyubimov AY, Lario PI, Moustafa I, Vrielink A. Atomic resolution crystallography reveals how changes in pH shape the protein microenvironment. Nat Chem Biol. 2006 May;2(5):259-64. Epub 2006 Apr 9. PMID:16604066 doi:10.1038/nchembio784

2gew, resolution 0.97Å

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=2gew&oldid=3850263"