1ibf: Difference between revisions
New page: left|200px<br /><applet load="1ibf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ibf, resolution 2.2Å" /> '''X-RAY 3D STRUCTURE OF... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1ibf.jpg|left|200px]]<br /><applet load="1ibf" size=" | [[Image:1ibf.jpg|left|200px]]<br /><applet load="1ibf" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1ibf, resolution 2.2Å" /> | caption="1ibf, resolution 2.2Å" /> | ||
'''X-RAY 3D STRUCTURE OF P.LEIOGNATHI CU,ZN SOD MUTANT V29G'''<br /> | '''X-RAY 3D STRUCTURE OF P.LEIOGNATHI CU,ZN SOD MUTANT V29G'''<br /> | ||
==Overview== | ==Overview== | ||
The functional properties and X-ray structures of five mutant forms of | 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. | ||
==About this Structure== | ==About this Structure== | ||
1IBF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Photobacterium_leiognathi Photobacterium leiognathi] with ZN and CU as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] Full crystallographic information is available from [http:// | 1IBF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Photobacterium_leiognathi Photobacterium leiognathi] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=CU:'>CU</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IBF OCA]. | ||
==Reference== | ==Reference== | ||
| Line 19: | Line 19: | ||
[[Category: Desideri, A.]] | [[Category: Desideri, A.]] | ||
[[Category: Milani, M.]] | [[Category: Milani, M.]] | ||
[[Category: Neill, P | [[Category: Neill, P O.]] | ||
[[Category: Orazio, M | [[Category: Orazio, M D.]] | ||
[[Category: Pesce, A.]] | [[Category: Pesce, A.]] | ||
[[Category: Rosano, C.]] | [[Category: Rosano, C.]] | ||
[[Category: Stroppolo, M | [[Category: Stroppolo, M E.]] | ||
[[Category: CU]] | [[Category: CU]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
| Line 29: | Line 29: | ||
[[Category: subunit interaction]] | [[Category: subunit interaction]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:10:01 2008'' | ||
Revision as of 14:10, 21 February 2008
|
X-RAY 3D STRUCTURE OF P.LEIOGNATHI CU,ZN SOD MUTANT V29G
OverviewOverview
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.
About this StructureAbout this Structure
1IBF is a Single protein structure of sequence from Photobacterium leiognathi with and as ligands. Active as Superoxide dismutase, with EC number 1.15.1.1 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
Page seeded by OCA on Thu Feb 21 13:10:01 2008