1udd: Difference between revisions

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[[Image:1udd.~~jpg~~|left|200px]]

[[Image:1udd.png|left|200px]]

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~~'''~~TenA homologue protein from P.horikoshii OT3~~'''~~

===TenA homologue protein from P.horikoshii OT3===

~~==Overview==~~

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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~~.

The line below this paragraph, {{ABSTRACT_PUBMED_15159569}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 15159569 is the PubMed ID number.

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==About this Structure==

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[[Category: Yao, M.]]

[[Category: Helix-bundle]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 11~~:04:07 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:19:30 2008''

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-[[Image:1udd.jpg|left|200px]]
+{{Seed}}
+[[Image:1udd.png|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===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15159569}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15159569 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15159569}}
 ==About this Structure==
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 [[Category: Yao, M.]]
 [[Category: Helix-bundle]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 11:04:07 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:19:30 2008''