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1OJL

Crystal structure of a sigma54-activator suggests the mechanism for the conformational switch necessary for sigma54 binding

Summary for 1OJL
Entry DOI10.2210/pdb1ojl/pdb
DescriptorTRANSCRIPTIONAL REGULATORY PROTEIN ZRAR, PHOSPHATE ION, ADENOSINE-5'-TRIPHOSPHATE, ... (4 entities in total)
Functional Keywordsresponse regulator, two component system, aaa domain, ntrc family, dna-binding, transcription regulation
Biological sourceSALMONELLA TYPHIMURIUM
Total number of polymer chains6
Total formula weight203413.62
Authors
Sallai, L.,Tucker, P.A. (deposition date: 2003-07-10, release date: 2005-05-19, Last modification date: 2024-05-08)
Primary citationSallai, L.,Tucker, P.A.
Crystal structure of the central and C-terminal domain of the sigma(54)-activator ZraR.
J. Struct. Biol., 151:160-170, 2005
Cited by
PubMed Abstract: 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.
PubMed: 16005641
DOI: 10.1016/j.jsb.2005.05.006
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

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