We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1ojl

From Proteopedia

Jump to: navigation, search

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

Structural highlights

1ojl is a 6 chain structure with sequence from Salmonella enterica subsp. enterica serovar Typhimurium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ZRAR_SALTY Member of the two-component regulatory system ZraS/ZraR. When activated by ZraS it acts in conjunction with sigma-54 to regulate the expression of zraP. Positively autoregulates the expression of the zraSR operon (By similarity).

Evolutionary Conservation

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