This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2zbx

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px <!-- The line below this paragraph, containing "STRUCTURE_2zbx", creates the "Structure Box" on the page. You may change the PDB parameter (which sets the PD...)
Line 1: Line 1:
-
[[Image:2zbx.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2zbx.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2zbx| PDB=2zbx | SCENE= }}
{{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.
 +
-->
 +
{{ABSTRACT_PUBMED_18314962}}
==About this Structure==
==About this Structure==
Line 39: Line 43:
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: P450]]
[[Category: P450]]
 +
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:31:11 2008''

Revision as of 21:31, 27 July 2008

Template:STRUCTURE 2zbx

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

Template:ABSTRACT PUBMED 18314962

About this Structure

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

Reference

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?)

OCA

Personal tools