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Structure and function of mutationally generated monomers of dimeric phosphoribosylanthranilate isomerase from Thermotoga maritima.

Thoma, Ralf, Hennig, Michael, Sterner, Reinhard and Kirschner, Kasper (2000) Structure and function of mutationally generated monomers of dimeric phosphoribosylanthranilate isomerase from Thermotoga maritima. Structure (London, England : 1993) 8 (3), pp. 265-76.

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Abstract

BACKGROUND: Oligomeric proteins may have been selected for in hyperthermophiles because subunit association provides extra stabilization. Phosphoribosylanthranilate isomerase (PRAI) is monomeric and labile in most mesophilic microorganisms, but dimeric and stable in the hyperthermophile Thermotoga maritima (tPRAI). The two subunits of tPRAI are associated back-to-back and are locked together by a ...

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Item type:Article
Date:2000
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Reinhard Sterner
Identification Number:
ValueType
10745009PubMed ID
Classification:
NotationType
Aldose-Ketose Isomerases/metabolismMESH
Base SequenceMESH
Crystallography, X-RayMESH
DNA PrimersMESH
DimerizationMESH
Evolution, MolecularMESH
Models, MolecularMESH
Structure-Activity RelationshipMESH
Thermotoga maritima/enzymologyMESH
Dewey Decimal Classification:500 Science > 570 Life sciences
Status:Published
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:Yes
Item ID:13704
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