2ce4
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The structure of the manganese superoxide dismutase (Mn-SOD; DR1279) from, Deinococcus radiodurans has been determined in two different crystal, forms. Both crystal forms are monoclinic with space group P2(1). Form I, has unit-cell parameters a = 44.28, b = 83.21, c = 59.52 angstroms, beta =, 110.18 degrees and contains a homodimer in the asymmetric unit, with, structure refinement (R = 16.8%, R(free) = 23.6%) carried out using data, to d(min) = 2.2 angstroms. Form II has unit-cell parameters a = 43.57, b =, 87.10, c = 116.42 angstroms, beta = 92.1 degrees and an asymmetric unit, containing two Mn-SOD homodimers; structure refinement was effected to a, resolution of 2.0 angstroms (R = 17.2%, R(free) = 22.3%). The resulting, structures are compared with that of Mn-SOD from Escherichia . | + | The structure of the manganese superoxide dismutase (Mn-SOD; DR1279) from, Deinococcus radiodurans has been determined in two different crystal, forms. Both crystal forms are monoclinic with space group P2(1). Form I, has unit-cell parameters a = 44.28, b = 83.21, c = 59.52 angstroms, beta =, 110.18 degrees and contains a homodimer in the asymmetric unit, with, structure refinement (R = 16.8%, R(free) = 23.6%) carried out using data, to d(min) = 2.2 angstroms. Form II has unit-cell parameters a = 43.57, b =, 87.10, c = 116.42 angstroms, beta = 92.1 degrees and an asymmetric unit, containing two Mn-SOD homodimers; structure refinement was effected to a, resolution of 2.0 angstroms (R = 17.2%, R(free) = 22.3%). The resulting, structures are compared with that of Mn-SOD from Escherichia coli, with, which they are shown to be essentially isostructural. |
==About this Structure== | ==About this Structure== | ||
| - | 2CE4 is a | + | 2CE4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans] with MN 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] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CE4 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: radiation resistance]] | [[Category: radiation resistance]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:52:25 2007'' |
Revision as of 12:47, 5 November 2007
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MANGANESE SUPEROXIDE DISMUTASE (MN-SOD) FROM DEINOCOCCUS RADIODURANS
Overview
The structure of the manganese superoxide dismutase (Mn-SOD; DR1279) from, Deinococcus radiodurans has been determined in two different crystal, forms. Both crystal forms are monoclinic with space group P2(1). Form I, has unit-cell parameters a = 44.28, b = 83.21, c = 59.52 angstroms, beta =, 110.18 degrees and contains a homodimer in the asymmetric unit, with, structure refinement (R = 16.8%, R(free) = 23.6%) carried out using data, to d(min) = 2.2 angstroms. Form II has unit-cell parameters a = 43.57, b =, 87.10, c = 116.42 angstroms, beta = 92.1 degrees and an asymmetric unit, containing two Mn-SOD homodimers; structure refinement was effected to a, resolution of 2.0 angstroms (R = 17.2%, R(free) = 22.3%). The resulting, structures are compared with that of Mn-SOD from Escherichia coli, with, which they are shown to be essentially isostructural.
About this Structure
2CE4 is a Single protein structure of sequence from Deinococcus radiodurans with MN as ligand. Active as Superoxide dismutase, with EC number 1.15.1.1 Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
Structure of the manganese superoxide dismutase from Deinococcus radiodurans in two crystal forms., Dennis RJ, Micossi E, McCarthy J, Moe E, Gordon EJ, Kozielski-Stuhrmann S, Leonard GA, McSweeney S, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2006 Apr 1;62(Pt, 4):325-9. Epub 2006 Mar 25. PMID:16582477
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