1e5s: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
[[Image:1e5s.gif|left|200px]]
{{Seed}}
[[Image:1e5s.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1e5s|  PDB=1e5s  |  SCENE=  }}  
{{STRUCTURE_1e5s|  PDB=1e5s  |  SCENE=  }}  


'''PROLINE 3-HYDROXYLASE (TYPE II)-IRON FORM'''
===PROLINE 3-HYDROXYLASE (TYPE II)-IRON FORM===




==Overview==
<!--  
Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases catalyse oxidative reactions in a range of metabolic processes including the hydroxylation of proline and lysine residues during the post-translational modification of collagen. 2-OG oxygenases commonly require ascorbate for full activity. In the vitamin C deficient disease, scurvy, reduced activity of 2-OG oxygenases results in impaired formation of collagen. Here we report the crystal structure of bacterial proline 3-hydroxylase from Streptomyces sp., an enzyme which hydroxylates proline at position 3, the first of a 2-OG oxygenase catalysing oxidation of a free alpha-amino acid. Structures were obtained for the enzyme in the absence of iron (to 2.3A resolution, R=20.2%, Rfree=25.3%) and that complexed to iron (II) (to 2.4A resolution, R=19.8%, Rfree=22.6%). The structure contains conserved motifs present in other 2-OG oxygenases including a 'jelly roll' beta strand core and residues binding iron and 2-oxoglutarate, consistent with divergent evolution within the extended family. The structure differs significantly from many other 2-OG oxygenases in possessing a discrete C-terminal helical domain. Analysis of the structure suggests a model for proline binding and a mechanism for uncoupling of proline and 2-OG turnover.
The line below this paragraph, {{ABSTRACT_PUBMED_11737217}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 11737217 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_11737217}}


==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Schofield, C J.]]
[[Category: Schofield, C J.]]
[[Category: 2-oxoglutarate dependent oxygenase]]
[[Category: 2-oxoglutarate dependent oxygenase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:42:00 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:11:44 2008''