1qo2

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File:1qo2.gif


1qo2, resolution 1.85Å

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CRYSTAL STRUCTURE OF N-((5'-PHOSPHORIBOSYL)-FORMIMINO)-5-AMINOIMIDAZOL-4-CARBOXAMID RIBONUCLEOTID ISOMERASE (EC 3.1.3.15, HISA)

OverviewOverview

The atomic structures of two proteins in the histidine biosynthesis pathway consist of beta/alpha barrels with a twofold repeat pattern. It is likely that these proteins evolved by twofold gene duplication and gene fusion from a common half-barrel ancestor. These ancestral domains are not visible as independent domains in the extant proteins but can be inferred from a combination of sequence and structural analysis. The detection of subdomain structures may be useful in efforts to search genome sequences for functionally and structurally related proteins.

About this StructureAbout this Structure

1QO2 is a Single protein structure of sequence from Thermotoga maritima. Active as D-lyxose ketol-isomerase, with EC number 5.3.1.15 Full crystallographic information is available from OCA.

ReferenceReference

Structural evidence for evolution of the beta/alpha barrel scaffold by gene duplication and fusion., Lang D, Thoma R, Henn-Sax M, Sterner R, Wilmanns M, Science. 2000 Sep 1;289(5484):1546-50. PMID:10968789

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