2i0k

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[[Image:2i0k.jpg|left|200px]]<br /><applet load="2i0k" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2i0k.jpg|left|200px]]
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caption="2i0k, resolution 1.60&Aring;" />
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'''Cholesterol Oxidase from Brevibacterium sterolicum- His121Ala Mutant'''<br />
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{{Structure
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|PDB= 2i0k |SIZE=350|CAPTION= <scene name='initialview01'>2i0k</scene>, resolution 1.60&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''Cholesterol Oxidase from Brevibacterium sterolicum- His121Ala Mutant'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2I0K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Brevibacterium_sterolicum Brevibacterium sterolicum] with <scene name='pdbligand=MN:'>MN</scene>, <scene name='pdbligand=CAC:'>CAC</scene>, <scene name='pdbligand=FAD:'>FAD</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=2I0K OCA].
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2I0K is a [[Single protein]] structure of 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=2I0K OCA].
==Reference==
==Reference==
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Structural and kinetic analyses of the H121A mutant of cholesterol oxidase., Lim L, Molla G, Guinn N, Ghisla S, Pollegioni L, Vrielink A, Biochem J. 2006 Nov 15;400(1):13-22. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16856877 16856877]
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Structural and kinetic analyses of the H121A mutant of cholesterol oxidase., Lim L, Molla G, Guinn N, Ghisla S, Pollegioni L, Vrielink A, Biochem J. 2006 Nov 15;400(1):13-22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16856877 16856877]
[[Category: Brevibacterium sterolicum]]
[[Category: Brevibacterium sterolicum]]
[[Category: Cholesterol oxidase]]
[[Category: Cholesterol oxidase]]
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[[Category: oxidoreductase]]
[[Category: oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:47:47 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:24:04 2008''

Revision as of 15:24, 20 March 2008

Image:2i0k.jpg


PDB ID 2i0k

Drag the structure with the mouse to rotate
, resolution 1.60Å
Ligands: , , and
Activity: Cholesterol oxidase, with EC number 1.1.3.6
Coordinates: save as pdb, mmCIF, xml



Cholesterol Oxidase from Brevibacterium sterolicum- His121Ala Mutant


Overview

Cholesterol oxidase is a monomeric flavoenzyme that catalyses the oxidation of cholesterol to cholest-5-en-3-one followed by isomerization to cholest-4-en-3-one. The enzyme from Brevibacterium sterolicum contains the FAD cofactor covalently bound to His121. It was previously demonstrated that the H121A substitution results in a approximately 100 mV decrease in the midpoint redox potential and a approximately 40-fold decrease in turnover number compared to wild-type enzyme [Motteran, Pilone, Molla, Ghisla and Pollegioni (2001) Journal of Biological Chemistry 276, 18024-18030]. A detailed kinetic analysis of the H121A mutant enzyme shows that the decrease in turnover number is largely due to a corresponding decrease in the rate constant of flavin reduction, whilst the re-oxidation reaction is only marginally altered and the isomerization reaction is not affected by the substitution and precedes product dissociation. The X-ray structure of the mutant protein, determined to 1.7 A resolution (1 A identical with 0.1 nm), reveals only minor changes in the overall fold of the protein, namely: two loops have slight movements and a tryptophan residue changes conformation by a rotation of 180 degrees about chi1 compared to the native enzyme. Comparison of the isoalloxazine ring moiety of the FAD cofactor between the structures of the native and mutant proteins shows a change from a non-planar to a planar geometry (resulting in a more tetrahedral-like geometry for N5). This change is proposed to be a major factor contributing to the observed alteration in redox potential. Since a similar distortion of the flavin has not been observed in other covalent flavoproteins, it is proposed to represent a specific mode to facilitate flavin reduction in covalent cholesterol oxidase.

About this Structure

2I0K is a Single protein structure of sequence from Brevibacterium sterolicum. Full crystallographic information is available from OCA.

Reference

Structural and kinetic analyses of the H121A mutant of cholesterol oxidase., Lim L, Molla G, Guinn N, Ghisla S, Pollegioni L, Vrielink A, Biochem J. 2006 Nov 15;400(1):13-22. PMID:16856877

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