Publication Date:
2000-09-01
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lang, D -- Thoma, R -- Henn-Sax, M -- Sterner, R -- Wilmanns, M -- New York, N.Y. -- Science. 2000 Sep 1;289(5484):1546-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉European Molecular Biology Laboratory (EMBL) Hamburg Outstation, EMBL c/o Deutsches Elektronen- Synchrotron (DESY), Notkestrasse 85, D-22603 Hamburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10968789" target="_blank"〉PubMed〈/a〉
Keywords:
Aldose-Ketose Isomerases/*chemistry/genetics/metabolism
;
Amino Acid Motifs
;
Amino Acid Sequence
;
Aminohydrolases/*chemistry/genetics/metabolism
;
Binding Sites
;
Catalysis
;
Crystallography, X-Ray
;
*Evolution, Molecular
;
*Gene Duplication
;
Histidine/biosynthesis
;
Models, Molecular
;
Molecular Sequence Data
;
Protein Folding
;
*Protein Structure, Tertiary
;
*Recombination, Genetic
;
Sequence Alignment
;
Thermotoga maritima/enzymology
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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