1udd: Difference between revisions
New page: left|200px<br /><applet load="1udd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1udd, resolution 2.15Å" /> '''TenA homologue prote... |
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[[Image:1udd.jpg|left|200px]]<br /><applet load="1udd" size=" | [[Image:1udd.jpg|left|200px]]<br /><applet load="1udd" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1udd, resolution 2.15Å" /> | caption="1udd, resolution 2.15Å" /> | ||
'''TenA homologue protein from P.horikoshii OT3'''<br /> | '''TenA homologue protein from P.horikoshii OT3'''<br /> | ||
==Overview== | ==Overview== | ||
The crystal structure of the Bacillus subtilis TenA-homologue protein | The crystal structure of the Bacillus subtilis TenA-homologue protein PH1161 from the hyperthermophilic archaebacterium Pyrococcus horikoshii was determined. TenA is known to belong to a new family of activators that stimulate the production of extracellular proteases in B. subtilis. A sequence-similarity search revealed that TenA-homologue proteins are widespread in bacteria and archaea, suggesting that this family of proteins plays an essential role in these organisms. In the present study, the first three-dimensional structure of a member of the TenA family of proteins was determined, unexpectedly revealing that the protein has a fold identical to that of haem oxygenase-1. Analysis has also shown that the protein has a unique ligand-binding pocket. Electron density of a bound ligand molecule was observed in this pocket. These results provide a valuable insight into the functional understanding of the TenA family of proteins. | ||
==About this Structure== | ==About this Structure== | ||
1UDD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http:// | 1UDD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UDD OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: helix-bundle]] | [[Category: helix-bundle]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:23:17 2008'' | ||
Revision as of 16:23, 21 February 2008
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TenA homologue protein from P.horikoshii OT3
OverviewOverview
The crystal structure of the Bacillus subtilis TenA-homologue protein PH1161 from the hyperthermophilic archaebacterium Pyrococcus horikoshii was determined. TenA is known to belong to a new family of activators that stimulate the production of extracellular proteases in B. subtilis. A sequence-similarity search revealed that TenA-homologue proteins are widespread in bacteria and archaea, suggesting that this family of proteins plays an essential role in these organisms. In the present study, the first three-dimensional structure of a member of the TenA family of proteins was determined, unexpectedly revealing that the protein has a fold identical to that of haem oxygenase-1. Analysis has also shown that the protein has a unique ligand-binding pocket. Electron density of a bound ligand molecule was observed in this pocket. These results provide a valuable insight into the functional understanding of the TenA family of proteins.
About this StructureAbout this Structure
1UDD is a Single protein structure of sequence from Pyrococcus horikoshii. Full crystallographic information is available from OCA.
ReferenceReference
Structure analysis of PH1161 protein, a transcriptional activator TenA homologue from the hyperthermophilic archaeon Pyrococcus horikoshii., Itou H, Yao M, Watanabe N, Tanaka I, Acta Crystallogr D Biol Crystallogr. 2004 Jun;60(Pt 6):1094-100. Epub 2004, May 21. PMID:15159569
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