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1wb8

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[[Image:1wb8.gif|left|200px]]
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{{STRUCTURE_1wb8| PDB=1wb8 | SCENE= }}
{{STRUCTURE_1wb8| PDB=1wb8 | SCENE= }}
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'''IRON SUPEROXIDE DISMUTASE (FE-SOD) FROM THE HYPERTHERMOPHILE SULFOLOBUS SOLFATARICUS. 2.3 A RESOLUTION STRUCTURE OF RECOMBINANT PROTEIN WITH A COVALENTLY MODIFIED TYROSIN IN THE ACTIVE SITE.'''
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===IRON SUPEROXIDE DISMUTASE (FE-SOD) FROM THE HYPERTHERMOPHILE SULFOLOBUS SOLFATARICUS. 2.3 A RESOLUTION STRUCTURE OF RECOMBINANT PROTEIN WITH A COVALENTLY MODIFIED TYROSIN IN THE ACTIVE SITE.===
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==Overview==
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The crystal structure of superoxide dismutase (SOD) from the hyper thermophile Sulfolobus solfataricus has been determined at 2.3 A resolution by molecular replacement and refined to a crystallographic R-factor of 16.8 % (Rfree 19.8 %). The crystals belong to the space group C2 (a=76.3 A, b=124.3 A, c=60.3 A, beta=128.8 degrees) with two identical monomers in the asymmetric unit. The monomer has a molecular weight of 24 kDa and consists of 210 amino acid residues of which 205 are visible in the electron density map. The overall fold of the monomer of S. solfataricus SOD is similar to that of the other known Fe or Mn-SODs. S. solfataricus SOD forms a very compact tetramer of a type similar to that of SOD from the hyperthermophile Aquifex pyrophilus. Both structures show an elevated number of inter-subunit ion-pairs compared with the mesophilic SOD from Mycobacterium tuberculosis and the thermophilic SOD from Thermus thermophilus. However, in contrast to the A. pyrophilus SOD structure, the number of intra-subunit ion-pairs as well as inter- subunit hydrogen bonds is not higher than in the compared mesophilic and thermophilic SOD structures. The electron density also revealed an unexpected and unusual covalent modification of a conserved tyrosine in the active site. Its involvement in the specific activity of the enzyme is discussed.
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(as it appears on PubMed at http://www.pubmed.gov), where 9931259 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9931259}}
==About this Structure==
==About this Structure==
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[[Category: Superoxide radical disproportionation]]
[[Category: Superoxide radical disproportionation]]
[[Category: Thermostable]]
[[Category: Thermostable]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:24:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:24:25 2008''

Revision as of 00:24, 29 July 2008

Image:1wb8.png

Template:STRUCTURE 1wb8

IRON SUPEROXIDE DISMUTASE (FE-SOD) FROM THE HYPERTHERMOPHILE SULFOLOBUS SOLFATARICUS. 2.3 A RESOLUTION STRUCTURE OF RECOMBINANT PROTEIN WITH A COVALENTLY MODIFIED TYROSIN IN THE ACTIVE SITE.

Template:ABSTRACT PUBMED 9931259

About this Structure

1WB8 is a Single protein structure of sequence from Sulfolobus solfataricus. This structure supersedes the now removed PDB entry 1sss. Full crystallographic information is available from OCA.

Reference

Iron superoxide dismutase from the archaeon Sulfolobus solfataricus: analysis of structure and thermostability., Ursby T, Adinolfi BS, Al-Karadaghi S, De Vendittis E, Bocchini V, J Mol Biol. 1999 Feb 12;286(1):189-205. PMID:9931259

Page seeded by OCA on Tue Jul 29 03:24:25 2008

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