1qo2: Difference between revisions
New page: left|200px<br /><applet load="1qo2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qo2, resolution 1.85Å" /> '''CRYSTAL STRUCTURE OF... |
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[[Image:1qo2.gif|left|200px]]<br /><applet load="1qo2" size=" | [[Image:1qo2.gif|left|200px]]<br /><applet load="1qo2" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1qo2, resolution 1.85Å" /> | caption="1qo2, resolution 1.85Å" /> | ||
'''CRYSTAL STRUCTURE OF N-((5'-PHOSPHORIBOSYL)-FORMIMINO)-5-AMINOIMIDAZOL-4-CARBOXAMID RIBONUCLEOTID ISOMERASE (EC 3.1.3.15, HISA)'''<br /> | '''CRYSTAL STRUCTURE OF N-((5'-PHOSPHORIBOSYL)-FORMIMINO)-5-AMINOIMIDAZOL-4-CARBOXAMID RIBONUCLEOTID ISOMERASE (EC 3.1.3.15, HISA)'''<br /> | ||
==Overview== | ==Overview== | ||
The atomic structures of two proteins in the histidine biosynthesis | 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== | ==About this Structure== | ||
1QO2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Active as [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] Full crystallographic information is available from [http:// | 1QO2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QO2 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: thermophilic protein]] | [[Category: thermophilic protein]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:41:58 2008'' | ||
Revision as of 15:41, 21 February 2008
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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. Active as D-lyxose ketol-isomerase, with EC number 5.3.1.15 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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