1qo2: Difference between revisions
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|PDB= 1qo2 |SIZE=350|CAPTION= <scene name='initialview01'>1qo2</scene>, resolution 1.85Å | |PDB= 1qo2 |SIZE=350|CAPTION= <scene name='initialview01'>1qo2</scene>, resolution 1.85Å | ||
|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/D-lyxose_ketol-isomerase D-lyxose ketol-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.15 5.3.1.15] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/D-lyxose_ketol-isomerase D-lyxose ketol-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.15 5.3.1.15] </span> | ||
|GENE= THISA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima]) | |GENE= THISA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qo2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qo2 OCA], [http://www.ebi.ac.uk/pdbsum/1qo2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qo2 RCSB]</span> | |||
}} | }} | ||
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[[Category: thermophilic protein]] | [[Category: thermophilic protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:16:35 2008'' | ||
Revision as of 23:16, 30 March 2008
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| , resolution 1.85Å | |||||||
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| Ligands: | |||||||
| Gene: | THISA (Thermotoga maritima) | ||||||
| Activity: | D-lyxose ketol-isomerase, with EC number 5.3.1.15 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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