1ojl: Difference between revisions

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[[Image:1ojl.gif|left|200px]]
{{Seed}}
[[Image:1ojl.png|left|200px]]


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{{STRUCTURE_1ojl|  PDB=1ojl  |  SCENE=  }}  
{{STRUCTURE_1ojl|  PDB=1ojl  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF A SIGMA54-ACTIVATOR SUGGESTS THE MECHANISM FOR THE CONFORMATIONAL SWITCH NECESSARY FOR SIGMA54 BINDING'''
===CRYSTAL STRUCTURE OF A SIGMA54-ACTIVATOR SUGGESTS THE MECHANISM FOR THE CONFORMATIONAL SWITCH NECESSARY FOR SIGMA54 BINDING===




==Overview==
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The sigma(54)-dependent transcription in bacteria is associated with various stress and growth conditions. Activators of the sigma(54) protein contain a central domain belonging to the AAA+ superfamily of ATPases, members of which function in diverse cellular processes in both prokaryotic and eukaryotic cells. We describe the X-ray structure of an N-terminal domain deletion of the ZraR protein from Salmonella typhimurium, which is a homologue of the general nitrogen regulatory protein NtrC, at 3A resolution. The structure reveals a hexameric ring that is typical for AAA+ containing proteins but which differs from the heptameric ring found in the crystal structure of the AAA+ domain of NtrC1 from Aquifex aeolicus. The dimerisation interface between DNA-binding domains observed in the crystal structure suggests that dodecamers, rather than hexamers, might be the functionally important oligomer.
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==About this Structure==
==About this Structure==
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[[Category: Transcription regulation]]
[[Category: Transcription regulation]]
[[Category: Two component system]]
[[Category: Two component system]]
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