1qo2
From Proteopedia
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| - | [[Image:1qo2.gif|left|200px]] | + | [[Image:1qo2.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF N-((5'-PHOSPHORIBOSYL)-FORMIMINO)-5-AMINOIMIDAZOL-4-CARBOXAMID RIBONUCLEOTID ISOMERASE (EC 3.1.3.15, HISA)''' | + | {{Structure |
| + | |PDB= 1qo2 |SIZE=350|CAPTION= <scene name='initialview01'>1qo2</scene>, resolution 1.85Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |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] | ||
| + | |GENE= THISA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima]) | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF N-((5'-PHOSPHORIBOSYL)-FORMIMINO)-5-AMINOIMIDAZOL-4-CARBOXAMID RIBONUCLEOTID ISOMERASE (EC 3.1.3.15, HISA)''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1QO2 is a [ | + | 1QO2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QO2 OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10968789 10968789] |
[[Category: D-lyxose ketol-isomerase]] | [[Category: D-lyxose ketol-isomerase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: thermophilic protein]] | [[Category: thermophilic protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:40:20 2008'' |
Revision as of 11:40, 20 March 2008
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| , resolution 1.85Å | |||||||
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| Gene: | THISA (Thermotoga maritima) | ||||||
| Activity: | D-lyxose ketol-isomerase, with EC number 5.3.1.15 | ||||||
| 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)
Overview
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 Structure
1QO2 is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 13:40:20 2008
