1e9o
From Proteopedia
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| - | [[Image:1e9o.jpg|left|200px]]<br /><applet load="1e9o" size=" | + | [[Image:1e9o.jpg|left|200px]]<br /><applet load="1e9o" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1e9o, resolution 1.85Å" /> | caption="1e9o, resolution 1.85Å" /> | ||
'''CRYSTAL STRUCTURE OF BOVINE SOD-1 OF 3'''<br /> | '''CRYSTAL STRUCTURE OF BOVINE SOD-1 OF 3'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1E9O is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with CU as [http://en.wikipedia.org/wiki/ligand ligand]. 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=AC4:Cu Binding Site For Residue B153'>AC4</scene>, <scene name='pdbsite=CU1:Cu Binding Site For Residue A152'>CU1</scene>, <scene name='pdbsite=CU2:Cu Binding Site For Residue A153'>CU2</scene> and <scene name='pdbsite=CU3:Cu Binding Site For Residue B152'>CU3</scene>. Full crystallographic information is available from [http:// | + | 1E9O is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=CU:'>CU</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=AC4:Cu+Binding+Site+For+Residue+B153'>AC4</scene>, <scene name='pdbsite=CU1:Cu+Binding+Site+For+Residue+A152'>CU1</scene>, <scene name='pdbsite=CU2:Cu+Binding+Site+For+Residue+A153'>CU2</scene> and <scene name='pdbsite=CU3:Cu+Binding+Site+For+Residue+B152'>CU3</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E9O OCA]. |
==Reference== | ==Reference== | ||
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[[Category: superoxide]] | [[Category: superoxide]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:38:34 2008'' |
Revision as of 07:38, 3 February 2008
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CRYSTAL STRUCTURE OF BOVINE SOD-1 OF 3
Overview
The structure of the catalytic site in one subunit of bovine CuZn, superoxide dismutase is shown to be highly variable. A series of crystal, structures at approximately 1.7 A have been determined using data, collected from different crystals. Several conformations are observed for, the copper site from one of the subunits. These conformations lie between, those expected for the Cu(II) and Cu(I) forms of the enzyme and may, represent a slow positional rearrangement of the Cu site during the, crystallisation process due to the presence of a trace reductant in the, mother liquor. These states perhaps indicate some functionally relevant, structural steps that ultimately result in the breakage of the imidazolate, bridge between the two metal sites.This behaviour is not observed for the, second subunit of the dimeric enzyme, which remains in the, five-coordinate, distorted square planar geometry in all cases. We suggest, that this asymmetric behaviour may be caused by the lack of mobility for, the Glu119-Leu142 loop region in the second subunit caused by crystal, contacts. This region forms one wall of the active-site cavity, and its, mobility has been suggested, via molecular dynamics studies, to be, important for the catalytic mechanism.
About this Structure
1E9O is a Protein complex structure of sequences from Bos taurus with as ligand. Active as Superoxide dismutase, with EC number 1.15.1.1 Known structural/functional Sites: , , and . Full crystallographic information is available from OCA.
Reference
Conformational variability of the Cu site in one subunit of bovine CuZn superoxide dismutase: the importance of mobility in the Glu119-Leu142 loop region for catalytic function., Hough MA, Strange RW, Hasnain SS, J Mol Biol. 2000 Nov 24;304(2):231-41. PMID:11080458
Page seeded by OCA on Sun Feb 3 09:38:34 2008
Categories: Bos taurus | Protein complex | Superoxide dismutase | Hasnain, S.S. | Hough, M.A. | CU | Asymmetry | Enzyme | Sod | Superoxide
