1ibb

<table><tr><td colspan='2'>[[1ibb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"photobacterium_leiognathi_subsp._leiognathi"_(boisvert_et_al._1967)_ast_and_dunlap_2004 "photobacterium leiognathi subsp. leiognathi" (boisvert et al. 1967) ast and dunlap 2004]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IBB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IBB FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1bzo|1bzo]], [[1ib5|1ib5]], [[1ibd|1ibd]], [[1ibf|1ibf]], [[1ibh|1ibh]]</div></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] </span></td></tr>

[[https://www.uniprot.org/uniprot/SODC_PHOLE SODC_PHOLE]] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:11327787</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1ibb" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Superoxide dismutase]]

[[Category: Battistoni, A]]

[[Category: Bolognesi, M]]

[[Category: Bordo, D]]

[[Category: Desideri, A]]

[[Category: Milani, M]]

[[Category: Neill, P O]]

[[Category: Orazio, M D]]

[[Category: Pesce, A]]

[[Category: Rosano, C]]

[[Category: Stroppolo, M E]]

[[Category: Subunit interaction]]