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1ojl
From Proteopedia
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|PDB= 1ojl |SIZE=350|CAPTION= <scene name='initialview01'>1ojl</scene>, resolution 3.0Å | |PDB= 1ojl |SIZE=350|CAPTION= <scene name='initialview01'>1ojl</scene>, resolution 3.0Å | ||
|SITE= <scene name='pdbsite=AC1:Po4+Binding+Site+For+Chain+D'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Po4+Binding+Site+For+Chain+D'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ojl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ojl OCA], [http://www.ebi.ac.uk/pdbsum/1ojl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ojl RCSB]</span> | ||
}} | }} | ||
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[[Category: Sallai, L.]] | [[Category: Sallai, L.]] | ||
[[Category: Tucker, P A.]] | [[Category: Tucker, P A.]] | ||
| - | [[Category: ATP]] | ||
| - | [[Category: PO4]] | ||
[[Category: aaa domain]] | [[Category: aaa domain]] | ||
[[Category: dna-binding]] | [[Category: dna-binding]] | ||
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[[Category: two component system]] | [[Category: two component system]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:46:14 2008'' |
Revision as of 19:46, 30 March 2008
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| , resolution 3.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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