2zbx: Difference between revisions

Revision as of 00:31, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2zbx.png

Template:STRUCTURE 2zbx

Crystal structure of vitamin D hydroxylase cytochrome P450 105A1 (wild type) with imidazole boundCrystal structure of vitamin D hydroxylase cytochrome P450 105A1 (wild type) with imidazole bound

Template:ABSTRACT PUBMED 18314962

About this StructureAbout this Structure

2ZBX is a Single protein structure of sequence from Streptomyces griseolus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal Structure of CYP105A1 (P450SU-1) in Complex with 1alpha,25-Dihydroxyvitamin D3(,)., Sugimoto H, Shinkyo R, Hayashi K, Yoneda S, Yamada M, Kamakura M, Ikushiro S, Shiro Y, Sakaki T, Biochemistry. 2008 Apr 1;47(13):4017-27. Epub 2008 Mar 4. PMID:18314962

Page seeded by OCA on Mon Jul 28 00:31:11 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_2zbx|  PDB=2zbx  |  SCENE=  }}
-'''Crystal structure of vitamin D hydroxylase cytochrome P450 105A1 (wild type) with imidazole bound'''
+===Crystal structure of vitamin D hydroxylase cytochrome P450 105A1 (wild type) with imidazole bound===
-==Overview==
+<!--
-Vitamin D 3 (VD 3), a prohormone in mammals, plays a crucial role in the maintenance of calcium and phosphorus concentrations in serum. Activation of VD 3 requires 25-hydroxylation in the liver and 1alpha-hydroxylation in the kidney by cytochrome P450 (CYP) enzymes. Bacterial CYP105A1 converts VD 3 into 1alpha,25-dihydroxyvitamin D 3 (1alpha,25(OH) 2D 3) in two independent reactions, despite its low sequence identity with mammalian enzymes (&lt;21% identity). The present study determined the crystal structures of a highly active mutant (R84A) of CYP105A1 from Streptomyces griseolus in complex and not in complex with 1alpha,25(OH) 2D 3. The compound 1alpha,25(OH) 2D 3 is positioned 11 A from the iron atom along the I helix within the pocket. A similar binding mode is observed in the structure of the human CYP2R1-VD 3 complex, indicating a common substrate-binding mechanism for 25-hydroxylation. A comparison with the structure of wild-type CYP105A1 suggests that the loss of two hydrogen bonds in the R84A mutant increases the adaptability of the B' and F helices, creating a transient binding site. Further mutational analysis of the active site reveals that 25- and 1alpha-hydroxylations share residues that participate in these reactions. These results provide the structural basis for understanding the mechanism of the two-step hydroxylation that activates VD 3.
+The line below this paragraph, {{ABSTRACT_PUBMED_18314962}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18314962 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_18314962}}
 ==About this Structure==
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 [[Category: Oxidoreductase]]
 [[Category: P450]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:31:11 2008''