1n4u
From Proteopedia
(New page: 200px<br /><applet load="1n4u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n4u, resolution 0.95Å" /> '''CHOLESTEROL OXIDASE ...) |
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| - | [[Image:1n4u.gif|left|200px]]<br /><applet load="1n4u" size=" | + | [[Image:1n4u.gif|left|200px]]<br /><applet load="1n4u" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1n4u, resolution 0.95Å" /> | caption="1n4u, resolution 0.95Å" /> | ||
'''CHOLESTEROL OXIDASE FROM STREPTOMYCES @ pH 4.5 (STREPTOMYCES SP. SA-COO)'''<br /> | '''CHOLESTEROL OXIDASE FROM STREPTOMYCES @ pH 4.5 (STREPTOMYCES SP. SA-COO)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Hydrogen atoms are a vital component of enzyme structure and function. In | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1N4U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_sp. Streptomyces sp.] with PO4, FAE, OXY and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 1N4U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_sp. Streptomyces sp.] with <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=FAE:'>FAE</scene>, <scene name='pdbligand=OXY:'>OXY</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N4U OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptomyces sp.]] | [[Category: Streptomyces sp.]] | ||
| - | [[Category: Lario, P | + | [[Category: Lario, P I.]] |
[[Category: Vrielink, A.]] | [[Category: Vrielink, A.]] | ||
[[Category: FAE]] | [[Category: FAE]] | ||
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[[Category: steroid metabolism]] | [[Category: steroid metabolism]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:02:17 2008'' |
Revision as of 12:02, 21 February 2008
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CHOLESTEROL OXIDASE FROM STREPTOMYCES @ pH 4.5 (STREPTOMYCES SP. SA-COO)
Overview
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.
About this Structure
1N4U is a Single protein structure of sequence from Streptomyces sp. with , , and as ligands. Active as Cholesterol oxidase, with EC number 1.1.3.6 Full crystallographic information is available from OCA.
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:16604066
Page seeded by OCA on Thu Feb 21 14:02:17 2008
