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1THF

CYCLASE SUBUNIT OF IMIDAZOLEGLYCEROLPHOSPHATE SYNTHASE FROM THERMOTOGA MARITIMA

Summary for 1THF
Entry DOI10.2210/pdb1thf/pdb
DescriptorHISF PROTEIN, PHOSPHATE ION (3 entities in total)
Functional Keywordsthermophile, tim-barrel, histidine biosynthesis, lyase, phosphate-binding sites
Biological sourceThermotoga maritima
Cellular locationCytoplasm: Q9X0C6
Total number of polymer chains1
Total formula weight27929.79
Authors
Lang, D.A.,Wilmanns, M. (deposition date: 1998-09-17, release date: 2000-07-14, Last modification date: 2024-02-14)
Primary citationLang, D.A.,Obmolova, G.,Thoma, R.,Kirschner, K.,Sterner, R.,Wilmanns, M.
Structural evidence for evolution of the beta/alpha barrel scaffold by gene duplication and fusion.
Science, 289:1546-1550, 2000
Cited by
PubMed Abstract: 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.
PubMed: 10968789
DOI: 10.1126/science.289.5484.1546
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.45 Å)
Structure validation

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数据于2025-10-08公开中

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