1sos
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(New page: 200px<br /> <applet load="1sos" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sos, resolution 2.5Å" /> '''ATOMIC STRUCTURES OF...)
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Revision as of 17:10, 12 November 2007
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ATOMIC STRUCTURES OF WILD-TYPE AND THERMOSTABLE MUTANT RECOMBINANT HUMAN CU, ZN SUPEROXIDE DISMUTASE
Contents |
Overview
Superoxide dismutase enzymes protect aerobic organisms from, oxygen-mediated free-radical damage. Crystallographic structures of, recombinant human Cu,Zn superoxide dismutase have been determined, refined, and analyzed at 2.5 A resolution for wild-type and a designed, thermostable double-mutant enzyme (Cys-6----Ala, Cys-111----Ser). The 10, subunits (five dimers) in the crystallographic asymmetric unit form an, unusual stable open lattice with 80-A-diameter channels. The 10, independently fit and refined subunits provide high accuracy, error, analysis, and insights on loop conformations. There is a helix dipole, interaction with the Zn site, and 14 residues form two or more, structurally conserved side-chain to main-chain hydrogen bonds that appear, critical to active-site architecture, loop conformation, and the increased, stability resulting from the Cys-111----Ser mutation.
Disease
Known disease associated with this structure: Amyotrophic lateral sclerosis, due to SOD1 deficiency OMIM:[147450]
About this Structure
1SOS is a Single protein structure of sequence from Homo sapiens with CU, ZN, SO4 and ACE as ligands. The following page contains interesting information on the relation of 1SOS with [Superoxide Dismutase]. Active as Superoxide dismutase, with EC number 1.15.1.1 Full crystallographic information is available from OCA.
Reference
Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase., Parge HE, Hallewell RA, Tainer JA, Proc Natl Acad Sci U S A. 1992 Jul 1;89(13):6109-13. PMID:1463506
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