1mxt

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{{STRUCTURE_1mxt| PDB=1mxt | SCENE= }}
{{STRUCTURE_1mxt| PDB=1mxt | SCENE= }}
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'''Atomic resolution structure of Cholesterol oxidase (Streptomyces sp. SA-COO)'''
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===Atomic resolution structure of Cholesterol oxidase (Streptomyces sp. SA-COO)===
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==Overview==
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The crystal structure of cholesterol oxidase, a 56kDa flavoenzyme was anisotropically refined to 0.95A resolution. The final crystallographic R-factor and R(free) value is 11.0% and 13.2%, respectively. The quality of the electron density maps has enabled modeling of alternate conformations for 83 residues in the enzyme, many of which are located in the active site. The additional observed structural features were not apparent in the previous high-resolution structure (1.5A resolution) and have enabled the identification of a narrow tunnel leading directly to the isoalloxazine portion of the FAD prosthetic group. The hydrophobic nature of this narrow tunnel suggests it is the pathway for molecular oxygen to access the isoalloxazine group for the oxidative half reaction. Resolving the alternate conformations in the active site residues provides a model for the dynamics of substrate binding and a potential oxidation triggered gating mechanism involving access to the hydrophobic tunnel. This structure reveals that the NE2 atom of the active site histidine residue, H447, critical to the redox activity of this flavin oxidase, acts as a hydrogen bond donor rather than as hydrogen acceptor. The atomic resolution structure of cholesterol oxidase has revealed the presence of hydrogen atoms, dynamic aspects of the protein and how side-chain conformations are correlated with novel structural features such as the oxygen tunnel. This new structural information has provided us with the opportunity to re-analyze the roles played by specific residues in the mechanism of the enzyme.
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The line below this paragraph, {{ABSTRACT_PUBMED_12595270}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 12595270 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12595270}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Sub-atomic resolution crystal structure of cholesterol oxidase: what atomic resolution crystallography reveals about enzyme mechanism and the role of the FAD cofactor in redox activity., Lario PI, Sampson N, Vrielink A, J Mol Biol. 2003 Mar 7;326(5):1635-50. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12595270 12595270]
Sub-atomic resolution crystal structure of cholesterol oxidase: what atomic resolution crystallography reveals about enzyme mechanism and the role of the FAD cofactor in redox activity., Lario PI, Sampson N, Vrielink A, J Mol Biol. 2003 Mar 7;326(5):1635-50. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12595270 12595270]
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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: Cholesterol oxidase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: Steroid metabolism]]
[[Category: Steroid metabolism]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:50:56 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:03:54 2008''

Revision as of 10:03, 29 July 2008

Image:1mxt.png

Template:STRUCTURE 1mxt

Atomic resolution structure of Cholesterol oxidase (Streptomyces sp. SA-COO)

Template:ABSTRACT PUBMED 12595270

About this Structure

1MXT is a Single protein structure of sequence from Streptomyces sp.. Full crystallographic information is available from OCA.

Reference

Sub-atomic resolution crystal structure of cholesterol oxidase: what atomic resolution crystallography reveals about enzyme mechanism and the role of the FAD cofactor in redox activity., Lario PI, Sampson N, Vrielink A, J Mol Biol. 2003 Mar 7;326(5):1635-50. PMID:12595270

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

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