1bzo

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[[Image:1bzo.jpg|left|200px]]
[[Image:1bzo.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1bzo |SIZE=350|CAPTION= <scene name='initialview01'>1bzo</scene>, resolution 2.1&Aring;
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The line below this paragraph, containing "STRUCTURE_1bzo", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=IUM:URANYL+(VI)+ION'>IUM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1bzo| PDB=1bzo | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bzo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bzo OCA], [http://www.ebi.ac.uk/pdbsum/1bzo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bzo RCSB]</span>
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}}
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'''THREE-DIMENSIONAL STRUCTURE OF PROKARYOTIC CU,ZN SUPEROXIDE DISMUTASE FROM P.LEIOGNATHI, SOLVED BY X-RAY CRYSTALLOGRAPHY.'''
'''THREE-DIMENSIONAL STRUCTURE OF PROKARYOTIC CU,ZN SUPEROXIDE DISMUTASE FROM P.LEIOGNATHI, SOLVED BY X-RAY CRYSTALLOGRAPHY.'''
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[[Category: Rosano, C.]]
[[Category: Rosano, C.]]
[[Category: Stroppolo, M E.]]
[[Category: Stroppolo, M E.]]
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[[Category: monomeric cu]]
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[[Category: Monomeric cu]]
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[[Category: protein electrostatic]]
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[[Category: Protein electrostatic]]
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[[Category: protein-subunit recognition]]
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[[Category: Protein-subunit recognition]]
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[[Category: zn superoxide dismutase]]
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[[Category: Zn superoxide dismutase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:09:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:11:40 2008''
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Revision as of 09:09, 2 May 2008

Image:1bzo.jpg

Template:STRUCTURE 1bzo

THREE-DIMENSIONAL STRUCTURE OF PROKARYOTIC CU,ZN SUPEROXIDE DISMUTASE FROM P.LEIOGNATHI, SOLVED BY X-RAY CRYSTALLOGRAPHY.


Overview

Prokaryotic Cu,Zn superoxide dismutases are characterized by a distinct quaternary structure, as compared to that of the homologous eukaryotic enzymes. Here we report a newly determined crystal structure of the dimeric Cu,Zn superoxide dismutase from Photobacterium leiognathi (crystallized in space group R32, refined at 2.5 A resolution, R-factor 0.19) and analyse it in comparison with that of the monomeric enzyme from Escherichia coli. The dimeric assembly, observed also in a previously studied monoclinic crystal form of P. leiognathi Cu,Zn superoxide dismutase, is based on a ring-shaped subunit contact region, defining a solvated interface cavity. Three clusters of neighbouring residues play a direct role in the stabilization of the quaternary assembly. The present analysis, extended to the amino acid sequences of the other 11 known prokaryotic Cu,Zn superoxide dismutases, shows that at least in five other prokaryotic enzymes the interface residue clusters are under strong evolutionary constraint, suggesting the attainment of a quaternary structure coincident with that of P. leiognathi Cu,Zn superoxide dismutase. Calculation of electrostatic fields for both the enzymes from E. coli and P. leiognathi shows that the monomeric/dimeric association behaviour displayed by prokaryotic Cu, Zn superoxide dismutases is related to the distribution of surface charged residues. Moreover, Brownian dynamics simulations reproduce closely the observed enzyme:substrate association rates, highlighting the role of the active site neighbouring residues in determining the dismutase catalytic properties.

About this Structure

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

Reference

Evolutionary constraints for dimer formation in prokaryotic Cu,Zn superoxide dismutase., Bordo D, Matak D, Djinovic-Carugo K, Rosano C, Pesce A, Bolognesi M, Stroppolo ME, Falconi M, Battistoni A, Desideri A, J Mol Biol. 1999 Jan 8;285(1):283-96. PMID:9878406 Page seeded by OCA on Fri May 2 12:09:36 2008

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