Linked Life Data

9712831

Source:http://linkedlifedata.com/resource/pubmed/id/9712831

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
35
pubmed:dateCreated
1998-9-24
pubmed:abstractText
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. Point mutation of Glu170 --> Ala destabilizes the dimer structure, and the mutant protein occurs as a mixture of dimer and monomer species. The purified E170A MnSOD contains exclusively Fe and is devoid of superoxide dismutase activity. E170A Fe2-MnSOD closely resembles authentic FeSOD in terms of spectroscopic properties, anion interactions and pH titration behavior. Reconstitution of E170A Fe2-MnSOD with Mn(II) salts does not restore superoxide dismutase activity despite the spectroscopic similarity between E170A Mn2-MnSOD and wild type Mn2-MnSOD. Growth of sodA+ and sodA- E. coli containing the mutant plasmid pDT1-5(E170A) is impaired, suggesting that expression of mutant protein is toxic to the host cells.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
273
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
22188-93
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
A glutamate bridge is essential for dimer stability and metal selectivity in manganese superoxide dismutase.
pubmed:affiliation
Department of Biochemistry and Molecular Biology, Oregon Graduate Institute of Science and Technology, Portland, Oregon 97291-1000, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.