The structure of human mitochondrial manganese superoxide dismutase reveals a novel tetrameric interface of two 4-helix bundles

@article{Borgstahl1992TheSO,
  title={The structure of human mitochondrial manganese superoxide dismutase reveals a novel tetrameric interface of two 4-helix bundles},
  author={Gloria E. O. Borgstahl and Hans E. Parge and Michael J. Hickey and Wayne F. Beyer and R. A. Hallewell and John A. Tainer},
  journal={Cell},
  year={1992},
  volume={71},
  pages={107-118}
}
Amino Acid Substitution at the Dimeric Interface of Human Manganese Superoxide Dismutase*
TLDR
Compared with wild-type Mn-SOD, the site-specific mutants H30N, Y166F, and the corresponding double mutant showed 10-fold decreases in steady-state constants for catalysis measured by pulse radiolysis.
Subunit interaction in extracellular superoxide dismutase: Effects of mutations in the N‐terminal domain
TLDR
The N‐terminal domain of EC‐SOD has already been studied using the fusion protein FusNN, which forms a well‐defined three‐dimensional structure, which probably contains α‐helical elements and is responsible for the tetramerization of the protein.
Unique structural features of the monomeric Cu,Zn superoxide dismutase from Escherichia coli, revealed by X-ray crystallography.
TLDR
The first three-dimensional structure of a functional monomeric Cu, Zn superoxide dismutase (from Escherichia coli, E_SOD) is reported at 2.0 A resolution, suggesting a modified control of substrate steering toward the catalytic center.
Contribution of human manganese superoxide dismutase tyrosine 34 to structure and catalysis.
TLDR
Structural and catalytic roles of the highly conserved active-site residue Tyr34 are examined, based upon structure-function studies of MnSOD enzymes with mutations at this site, and an intermediate in catalysis is observed, which has not been reported previously.
Engineering of an intersubunit disulfide bridge in the iron-superoxide dismutase of Mycobacterium tuberculosis.
TLDR
The mutant protein was found to be less stable than the wild type as judged by susceptibility to denaturation in the presence of guanidine hydrochloride and decreased stability probably results from formation of a disulfide bridge with a suboptimal torsion angle and exclusion of solvent molecules from the dimer interface.
Nickel superoxide dismutase structure and mechanism.
TLDR
The 1.30 A resolution crystal structure of nickel superoxide dismutase (NiSOD) identifies a novel SOD fold, assembly, and Ni active site that provides almost all interactions critical for metal binding and catalysis, and thus will likely be diagnostic of NiSODs.
Role of a glutamate bridge spanning the dimeric interface of human manganese superoxide dismutase.
TLDR
Results suggest that Glu162 at the tetrameric interface in human MnSOD supports stability and efficient catalysis and has a significant role in regulating product inhibition.
A Glutamate Bridge Is Essential for Dimer Stability and Metal Selectivity in Manganese Superoxide Dismutase*
TLDR
In Escherichia coli manganese superoxide dismutase (MnSOD), the absolutely conserved Glu170 of one monomer is hydrogen-bonded to the Mn ligand His171 of the other monomer, forming a double bridge at the dimer interface, and the mutant protein occurs as a mixture of dimer and monomer species.
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TLDR
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).
Manganese and iron superoxide dismutases are structural homologs.
The crystal structure of a tetrameric manganese superoxide dismutase from a thermophilic bacterium, Thermus thermophilus HB8, has been determined at 4.4-A resolution by local averaging of electron
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TLDR
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TLDR
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TLDR
It is shown that site-specific mutants that increase local positive charge while maintaining this orienting network (Glu→Gin) have faster reaction rates and increased ionic-strength dependence, matching brownian dynamics simulations incorporating electrostatic terms.
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