1ibh: Difference between revisions

Revision as of 10:42, 1 July 2008

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File:1ibh.png

Template:STRUCTURE 1ibh

X-RAY 3D STRUCTURE OF P.LEIOGNATHI CU,ZN SOD MUTANT M41IX-RAY 3D STRUCTURE OF P.LEIOGNATHI CU,ZN SOD MUTANT M41I

Template:ABSTRACT PUBMED 11327787

About this StructureAbout this Structure

1IBH is a Single protein structure of sequence from Photobacterium leiognathi. Full crystallographic information is available from OCA.

ReferenceReference

Single mutations at the subunit interface modulate copper reactivity in Photobacterium leiognathi Cu,Zn superoxide dismutase., Stroppolo ME, Pesce A, D'Orazio M, O'Neill P, Bordo D, Rosano C, Milani M, Battistoni A, Bolognesi M, Desideri A, J Mol Biol. 2001 May 4;308(3):555-63. PMID:11327787

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OCA

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-'''X-RAY 3D STRUCTURE OF P.LEIOGNATHI CU,ZN SOD MUTANT M41I'''
+===X-RAY 3D STRUCTURE OF P.LEIOGNATHI CU,ZN SOD MUTANT M41I===
-==Overview==
+<!--
-The functional properties and X-ray structures of five mutant forms of Photobacterium leiognathi Cu,Zn superoxide dismutase carrying single mutations at residues located at the dimer association interface have been investigated. When compared to the wild-type enzyme, the three-dimensional structures of the mutants show structural perturbations limited to the proximity of the mutation sites and substantial identity of active site geometry. Nonetheless, the catalytic rates of all mutants, measured at neutral pH and low ionic strength by pulse radiolysis, are higher than that of the wild-type protein. Such enzymatic activity increase is paralleled by enhanced active site accessibility to external chelating agents, which, in the mutated enzyme, remove more readily the active site copper ion. It is concluded that mutations at the prokaryotic Cu,Zn superoxide dismutase subunit interface can transduce dynamical perturbation to the active site region, promoting substrate active site accessibility. Such long-range intramolecular communication effects have not been extensively described before within the Cu,Zn superoxide dismutase homology family.
+The line below this paragraph, {{ABSTRACT_PUBMED_11327787}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11327787 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_11327787}}
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 [[Category: Prokaryotic superoxide dismutase]]
 [[Category: Subunit interaction]]
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