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Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Sallai L, Tucker PA. Crystal structure of the central and C-terminal domain of the sigma(54)-activator ZraR. J Struct Biol. 2005 Aug;151(2):160-70. PMID:16005641 doi:10.1016/j.jsb.2005.05.006
