1yfu: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
Line 1: Line 1:
[[Image:1yfu.gif|left|200px]]
{{Seed}}
[[Image:1yfu.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1yfu|  PDB=1yfu  |  SCENE=  }}  
{{STRUCTURE_1yfu|  PDB=1yfu  |  SCENE=  }}  


'''Crystal structure of 3-hydroxyanthranilate-3,4-dioxygenase from Ralstonia metallidurans'''
===Crystal structure of 3-hydroxyanthranilate-3,4-dioxygenase from Ralstonia metallidurans===




==Overview==
<!--  
3-Hydroxyanthranilate-3,4-dioxygenase (HAD) catalyzes the oxidative ring opening of 3-hydroxyanthranilate in the final enzymatic step of the biosynthetic pathway from tryptophan to quinolinate, the universal de novo precursor to the pyridine ring of nicotinamide adenine dinucleotide. The enzyme requires Fe2+ as a cofactor and is inactivated by 4-chloro-3-hydroxyanthranilate. HAD from Ralstonia metallidurans was crystallized, and the structure was determined at 1.9 A resolution. The structures of HAD complexed with the inhibitor 4-chloro-3-hydroxyanthranilic acid and either molecular oxygen or nitric oxide were determined at 2.0 A resolution, and the structure of HAD complexed with 3-hydroxyanthranilate was determined at 3.2 A resolution. HAD is a homodimer with a subunit topology that is characteristic of the cupin barrel fold. Each monomer contains two iron binding sites. The catalytic iron is buried deep inside the beta-barrel with His51, Glu57, and His95 serving as ligands. The other iron site forms an FeS4 center close to the solvent surface in which the sulfur atoms are provided by Cys125, Cys128, Cys162, and Cys165. The two iron sites are separated by 24 A. On the basis of the crystal structures of HAD, mutagenesis studies were carried out in order to elucidate the enzyme mechanism. In addition, a new mechanism for the enzyme inactivation by 4-chloro-3-hydroxyanthranilate is proposed.
The line below this paragraph, {{ABSTRACT_PUBMED_15909978}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 15909978 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_15909978}}


==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Zhang, Y.]]
[[Category: Zhang, Y.]]
[[Category: Cupin]]
[[Category: Cupin]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 16:16:08 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:18:30 2008''

Revision as of 21:18, 27 July 2008

File:1yfu.png

Template:STRUCTURE 1yfu

Crystal structure of 3-hydroxyanthranilate-3,4-dioxygenase from Ralstonia metallidurans

Template:ABSTRACT PUBMED 15909978

About this Structure

1YFU is a Single protein structure of sequence from Cupriavidus metallidurans. Full crystallographic information is available from OCA.

Reference

Structural studies on 3-hydroxyanthranilate-3,4-dioxygenase: the catalytic mechanism of a complex oxidation involved in NAD biosynthesis., Zhang Y, Colabroy KL, Begley TP, Ealick SE, Biochemistry. 2005 May 31;44(21):7632-43. PMID:15909978

Page seeded by OCA on Mon Jul 28 00:18:30 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1yfu&oldid=673125"