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Dissection of a (betaalpha)8-barrel enzyme into two folded halves.

Höcker, Birte and Beismann-Driemeyer, Silke and Hettwer, Stefan and Lustig, A. and Sterner, Reinhard (2001) Dissection of a (betaalpha)8-barrel enzyme into two folded halves. Nature structural biology 8 (1), pp. 32-6.

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Abstract

The (betaalpha)8-barrel, which is the most frequently encountered protein fold, is generally considered to consist of a single structural domain. However, the X-ray structure of the imidazoleglycerol phosphate synthase (HisF) from Thermotoga maritima has identified it as a (betaalpha) 8-barrel made up of two superimposable subdomains (HisF-N and HisF-C). HisF-N consists of the four N-terminal ...

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Item Type:Article
Date:2001
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Reinhard Sterner
Identification Number:
ValueType
11135656PubMed ID
10.1038/83021DOI
Classification:
NotationType
Amino Acid SequenceMESH
Aminohydrolases/metabolismMESH
CatalysisMESH
Chromatography, GelMESH
Circular DichroismMESH
DimerizationMESH
Evolution, MolecularMESH
Gene DuplicationMESH
KineticsMESH
Models, MolecularMESH
Molecular Sequence DataMESH
Molecular WeightMESH
MutationMESH
Protein BindingMESH
Protein FoldingMESH
Protein Structure, SecondaryMESH
Protein Structure, TertiaryMESH
Recombinant Fusion Proteins/metabolismMESH
Sequence AlignmentMESH
ThermodynamicsMESH
Thermotoga maritima/geneticsMESH
UltracentrifugationMESH
Subjects:500 Science > 570 Life sciences
Status:Published
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:Yes
Owner: Universitätsbibliothek Regensburg
Deposited On:22 Mar 2010 08:53
Last Modified:22 Mar 2010 08:53
Item ID:13701
Owner Only: item control page
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