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1eso
From Proteopedia
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| - | [[Image:1eso.gif|left|200px]]<br /><applet load="1eso" size=" | + | [[Image:1eso.gif|left|200px]]<br /><applet load="1eso" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1eso, resolution 2.0Å" /> | caption="1eso, resolution 2.0Å" /> | ||
'''MONOMERIC CU,ZN SUPEROXIDE DISMUTASE FROM ESCHERICHIA COLI'''<br /> | '''MONOMERIC CU,ZN SUPEROXIDE DISMUTASE FROM ESCHERICHIA COLI'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ESO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] 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] Known structural/functional Sites: <scene name='pdbsite=CUL:Cu Ligands'>CUL</scene> and <scene name='pdbsite=ZNL:Zn Ligands'>ZNL</scene>. Full crystallographic information is available from [http:// | + | 1ESO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] 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] Known structural/functional Sites: <scene name='pdbsite=CUL:Cu+Ligands'>CUL</scene> and <scene name='pdbsite=ZNL:Zn+Ligands'>ZNL</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ESO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: zn superoxide dismutase]] | [[Category: zn superoxide dismutase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:39:27 2008'' |
Revision as of 07:39, 3 February 2008
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MONOMERIC CU,ZN SUPEROXIDE DISMUTASE FROM ESCHERICHIA COLI
Overview
The first three-dimensional structure of a functional monomeric Cu, Zn, superoxide dismutase (from Escherichia coli, E_SOD) is reported at 2.0 A, resolution (R-factor=16.8%). Compared to the homologous eukaryotic, enzymes, E_SOD displays a perturbed antiparallel beta-barrel structure., The most striking structural features observed include extended amino acid, insertions in the surface 1, 2-loop and S-S subloop, modification of the, disulfide bridge connection, and loss of functional electrostatic, residues, suggesting a modified control of substrate steering toward the, catalytic center. The active site Cu2+ displays a distorted coordination, sphere due to an unusually long bond to the metal-bridging residue His61., Inspection of the crystal packing does not show regions of extended, contact indicative of a dimeric assembly. The molecular surface region, involved in subunit dimerization in eukaryotic superoxide dismutases is, structurally altered in E_SOD and displays a net polar nature.
About this Structure
1ESO is a Single protein structure of sequence from Escherichia coli with and as ligands. Active as Superoxide dismutase, with EC number 1.15.1.1 Known structural/functional Sites: and . Full crystallographic information is available from OCA.
Reference
Unique structural features of the monomeric Cu,Zn superoxide dismutase from Escherichia coli, revealed by X-ray crystallography., Pesce A, Capasso C, Battistoni A, Folcarelli S, Rotilio G, Desideri A, Bolognesi M, J Mol Biol. 1997 Dec 5;274(3):408-20. PMID:9405149
Page seeded by OCA on Sun Feb 3 09:39:27 2008
Categories: Escherichia coli | Single protein | Superoxide dismutase | Battistoni, A. | Bolognesi, M. | Capasso, C. | Desideri, A. | Folcarelli, S. | Pesce, A. | Rotilio, G. | CU | ZN | Copper enzymes | Cu | Enzyme evolution | Monomeric superoxide dismutase | Oxidoreductase | X-ray crystal structure | Zn superoxide dismutase
