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

Structural highlights

1qo2 is a 2 chain structure with sequence from Atcc 43589. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Gene:THISA (ATCC 43589)
Activity:D-lyxose ketol-isomerase, with EC number 5.3.1.15
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum

Evolutionary Conservation

 

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

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

1qo2, resolution 1.85Å

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