1ibh: Difference between revisions
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|PDB= 1ibh |SIZE=350|CAPTION= <scene name='initialview01'>1ibh</scene>, resolution 2.0Å | |PDB= 1ibh |SIZE=350|CAPTION= <scene name='initialview01'>1ibh</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> | ||
|ACTIVITY= [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] | |ACTIVITY= <span class='plainlinks'>[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] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1bzo|1BZO]], [[1ib5|1IB5]], [[1ibb|1IBB]], [[1ibd|1IBD]], [[1ibf|1IBF]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ibh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ibh OCA], [http://www.ebi.ac.uk/pdbsum/1ibh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ibh RCSB]</span> | |||
}} | }} | ||
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[[Category: Rosano, C.]] | [[Category: Rosano, C.]] | ||
[[Category: Stroppolo, M E.]] | [[Category: Stroppolo, M E.]] | ||
[[Category: prokaryotic superoxide dismutase]] | [[Category: prokaryotic superoxide dismutase]] | ||
[[Category: subunit interaction]] | [[Category: subunit interaction]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:17:24 2008'' | ||
Revision as of 21:17, 30 March 2008
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| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Superoxide dismutase, with EC number 1.15.1.1 | ||||||
| Related: | 1BZO, 1IB5, 1IBB, 1IBD, 1IBF
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
X-RAY 3D STRUCTURE OF P.LEIOGNATHI CU,ZN SOD MUTANT M41I
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
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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