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1ojl
From Proteopedia
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CRYSTAL STRUCTURE OF A SIGMA54-ACTIVATOR SUGGESTS THE MECHANISM FOR THE CONFORMATIONAL SWITCH NECESSARY FOR SIGMA54 BINDING
Overview
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.
About this Structure
1OJL is a Single protein structure of sequence from Salmonella typhimurium with PO4 and ATP as ligands. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
Crystal structure of the central and C-terminal domain of the sigma(54)-activator ZraR., Sallai L, Tucker PA, J Struct Biol. 2005 Aug;151(2):160-70. PMID:16005641
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