1unf: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
Line 1: Line 1:
[[Image:1unf.jpg|left|200px]]
{{Seed}}
[[Image:1unf.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1unf|  PDB=1unf  |  SCENE=  }}  
{{STRUCTURE_1unf|  PDB=1unf  |  SCENE=  }}  


'''THE CRYSTAL STRUCTURE OF THE EUKARYOTIC FESOD FROM VIGNA UNGUICULATA SUGGESTS A NEW ENZYMATIC MECHANISM'''
===THE CRYSTAL STRUCTURE OF THE EUKARYOTIC FESOD FROM VIGNA UNGUICULATA SUGGESTS A NEW ENZYMATIC MECHANISM===




==Overview==
<!--
Superoxide dismutases (SODs) are a family of metalloenzymes that catalyze the dismutation of superoxide anion radicals into molecular oxygen and hydrogen peroxide. Iron superoxide dismutases (FeSODs) are only expressed in some prokaryotes and plants. A new and highly active FeSOD with an unusual subcellular localization has recently been isolated from the plant Vigna unguiculata (cowpea). This protein functions as a homodimer and, in contrast to the other members of the SOD family, is localized to the cytosol. The crystal structure of the recombinant enzyme has been solved and the model refined to 1.97 A resolution. The superoxide anion binding site is located in a cleft close to the dimer interface. The coordination geometry of the Fe site is a distorted trigonal bipyramidal arrangement, whose axial ligands are His43 and a solvent molecule, and whose in-plane ligands are His95, Asp195, and His199. A comparison of the structural features of cowpea FeSOD with those of homologous SODs reveals subtle differences in regard to the metal-protein interactions, and confirms the existence of two regions that may control the traffic of substrate and product: one located near the Fe binding site, and another in the dimer interface. The evolutionary conservation of reciprocal interactions of both monomers in neighboring active sites suggests possible subunit cooperation during catalysis.
The line below this paragraph, {{ABSTRACT_PUBMED_15659371}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 15659371 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_15659371}}


==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: Superoxide dismutase]]
[[Category: Superoxide dismutase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 11:27:54 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:17:20 2008''

Revision as of 13:17, 27 July 2008

File:1unf.png

Template:STRUCTURE 1unf

THE CRYSTAL STRUCTURE OF THE EUKARYOTIC FESOD FROM VIGNA UNGUICULATA SUGGESTS A NEW ENZYMATIC MECHANISM

Template:ABSTRACT PUBMED 15659371

About this Structure

1UNF is a Single protein structure of sequence from Vigna unguiculata. Full crystallographic information is available from OCA.

Reference

The crystal structure of an eukaryotic iron superoxide dismutase suggests intersubunit cooperation during catalysis., Munoz IG, Moran JF, Becana M, Montoya G, Protein Sci. 2005 Feb;14(2):387-94. PMID:15659371

Page seeded by OCA on Sun Jul 27 16:17:20 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1unf&oldid=655392"