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1KGS

Crystal Structure at 1.50 A of an OmpR/PhoB Homolog from Thermotoga maritima

Summary for 1KGS
Entry DOI10.2210/pdb1kgs/pdb
DescriptorDNA BINDING RESPONSE REGULATOR D, THIOCYANATE ION (3 entities in total)
Functional Keywordsdna-binding protein, alph-beta sandwich, winged-helix, helix-turn-helix, response regulator, dna binding protein
Biological sourceThermotoga maritima
Total number of polymer chains1
Total formula weight26826.85
Authors
Buckler, D.R.,Zhou, Y.,Stock, A.M. (deposition date: 2001-11-28, release date: 2001-12-05, Last modification date: 2024-10-16)
Primary citationBuckler, D.R.,Zhou, Y.,Stock, A.M.
Evidence of intradomain and interdomain flexibility in an OmpR/PhoB homolog from Thermotoga maritima.
Structure, 10:153-164, 2002
Cited by
PubMed Abstract: Two-component systems, the predominant signal transduction strategy used by prokaryotes, involve phosphorelay from a sensor histidine kinase (HK) to an intracellular response regulator protein (RR) that typically acts as a transcription regulator. RRs are modular proteins, usually composed of a conserved regulatory domain, which functions as a phosphorylation-activated switch, and an attached DNA binding effector domain. The crystal structure of a Thermotoga maritima transcription factor, DrrD, has been determined at 1.5 A resolution, providing the first structural information for a full-length member of the OmpR/PhoB subfamily of RRs. A small interdomain interface occurs between alpha 5 of the regulatory domain and an antiparallel sheet of the effector domain. The lack of an extensive interface in the unphosphorylated protein distinguishes DrrD from other structurally characterized multidomain RRs and suggests a different mode of interdomain regulation.
PubMed: 11839301
DOI: 10.1016/S0969-2126(01)00706-7
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.5 Å)
Structure validation

238582

数据于2025-07-09公开中

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