1sos: Difference between revisions
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'''ATOMIC STRUCTURES OF WILD-TYPE AND THERMOSTABLE MUTANT RECOMBINANT HUMAN CU, ZN SUPEROXIDE DISMUTASE''' | '''ATOMIC STRUCTURES OF WILD-TYPE AND THERMOSTABLE MUTANT RECOMBINANT HUMAN CU, ZN SUPEROXIDE DISMUTASE''' | ||
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[[Category: Parge, H E.]] | [[Category: Parge, H E.]] | ||
[[Category: Tainer, J A.]] | [[Category: Tainer, J A.]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:57:43 2008'' | |||
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Revision as of 08:57, 3 May 2008
ATOMIC STRUCTURES OF WILD-TYPE AND THERMOSTABLE MUTANT RECOMBINANT HUMAN CU, ZN SUPEROXIDE DISMUTASE
OverviewOverview
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.
About this StructureAbout this Structure
1SOS is a Single protein structure of sequence from Homo sapiens. The following page contains interesting information on the relation of 1SOS with [Superoxide Dismutase]. Full crystallographic information is available from OCA.
ReferenceReference
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 Page seeded by OCA on Sat May 3 08:57:43 2008