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1thf
From Proteopedia
| 1thf, resolution 1.45Å () | |||||||||
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| Ligands: | |||||||||
| Domains: | HisF, His_biosynth | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
CYCLASE SUBUNIT OF IMIDAZOLEGLYCEROLPHOSPHATE SYNTHASE FROM THERMOTOGA MARITIMA
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1THF is a 1 chain structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.
Reference
- 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
Page seeded by OCA on Wed Feb 18 05:21:01 2009
