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Structure paper

TitleMechanism of regulation of receptor histidine kinases.
Journal, issue, pagesStructure, Vol. 20, Page 56-66, Year 2012
Publish dateJul 10, 2011 (structure data deposition date)
AuthorsFerris, H.U. / Dunin-Horkawicz, S. / Hornig, N. / Hulko, M. / Martin, J. / Schultz, J.E. / Zeth, K. / Lupas, A.N. / Coles, M.
External linksStructure / PubMed:22244755
MethodsNMR (solution) / X-ray diffraction
Resolution1.25 - 2.25 Å
Structure data

PDB-2lfr:
Solution structure of the chimeric Af1503 HAMP- EnvZ DHp homodimer
Method: SOLUTION NMR

PDB-2lfs:
Solution structure of the chimeric Af1503 HAMP- EnvZ DHp homodimer; A219F variant
Method: SOLUTION NMR

PDB-3zrv:
The high resolution structure of a dimeric Hamp-Dhp fusion displays asymmetry - A291F mutant
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

PDB-3zrw:
The structure of the dimeric Hamp-Dhp fusion A291V mutant
Method: X-RAY DIFFRACTION / Resolution: 2.25 Å

PDB-3zrx:
The high resolution structure of a dimeric Hamp-Dhp fusion displays strong asymmetry
Method: X-RAY DIFFRACTION / Resolution: 1.25 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • archaeoglobus fulgidus (strain atcc 49558 / vc-16 / dsm 4304 / jcm 9628 / nbrc 100126) (archaea)
  • shigella flexneri (bacteria)
  • archaeoglobus fulgidus (archaea)
  • escherichia coli (E. coli)
KeywordsTRANSFERASE / transmembrane signaling / HAMP domain / histidine kinase / gearbox model / SIGNALING PROTEIN / SIGNALLING PROTEIN / HAMP / SIGNALLING / OSMOREGULATION / OMPR / OMPC

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