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[[Image:1udd.jpg|left|200px]]
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{{STRUCTURE_1udd|  PDB=1udd  |  SCENE=  }}
'''TenA homologue protein from P.horikoshii OT3'''


==TenA homologue protein from P.horikoshii OT3==
<StructureSection load='1udd' size='340' side='right'caption='[[1udd]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1udd]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii_OT3 Pyrococcus horikoshii OT3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UDD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UDD FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1udd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1udd OCA], [https://pdbe.org/1udd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1udd RCSB], [https://www.ebi.ac.uk/pdbsum/1udd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1udd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O58873_PYRHO O58873_PYRHO]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ud/1udd_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1udd ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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<ref>PMID:15159569</ref>
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==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1UDD is a [[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].
</div>
<div class="pdbe-citations 1udd" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/15159569 15159569]
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
[[Category: Pyrococcus horikoshii]]
== References ==
[[Category: Single protein]]
<references/>
[[Category: Itou, H.]]
__TOC__
[[Category: Tanaka, I.]]
</StructureSection>
[[Category: Watanabe, N.]]
[[Category: Large Structures]]
[[Category: Yao, M.]]
[[Category: Pyrococcus horikoshii OT3]]
[[Category: Helix-bundle]]
[[Category: Itou H]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 11:04:07 2008''
[[Category: Tanaka I]]
[[Category: Watanabe N]]
[[Category: Yao M]]

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