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Structure paper

TitleFull-length structure of a monomeric histidine kinase reveals basis for sensory regulation.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 111, Page 17839-17844, Year 2014
Publish dateAug 14, 2014 (structure data deposition date)
AuthorsRivera-Cancel, G. / Ko, W.H. / Tomchick, D.R. / Correa, F. / Gardner, K.H.
External linksProc. Natl. Acad. Sci. USA / PubMed:25468971
MethodsX-ray diffraction
Resolution1.6 - 2.92 Å
Structure data

PDB-4r38:
LOV domain from Erythrobacter litoralis EL346 blue-light activated histidine kinase
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-4r39:
Histidine kinase domain from Erythrobacter litoralis EL346 blue-light activated histidine kinase
Method: X-RAY DIFFRACTION / Resolution: 2.603 Å

PDB-4r3a:
Erythrobacter litoralis EL346 blue-light activated histidine kinase
Method: X-RAY DIFFRACTION / Resolution: 2.92 Å

Chemicals

ChemComp-RBF:
RIBOFLAVIN

ChemComp-HOH:
WATER

ChemComp-MG:
Unknown entry

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

Source
  • erythrobacter litoralis htcc2594 (bacteria)
KeywordsSIGNALING PROTEIN / riboflavin / light-activated / LOV domain / photoreceptor / sensory transduction / signal transduction / TRANSFERASE / histidine kinase domain / Bergerat fold / histidine kinase / cell signaling / regulation / two-component system

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