1kgs
From Proteopedia
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|PDB= 1kgs |SIZE=350|CAPTION= <scene name='initialview01'>1kgs</scene>, resolution 1.50Å | |PDB= 1kgs |SIZE=350|CAPTION= <scene name='initialview01'>1kgs</scene>, resolution 1.50Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SCN:THIOCYANATE ION'>SCN</scene> | + | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= DRRD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima]) | |GENE= DRRD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kgs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kgs OCA], [http://www.ebi.ac.uk/pdbsum/1kgs PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kgs RCSB]</span> | ||
}} | }} | ||
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[[Category: Stock, A M.]] | [[Category: Stock, A M.]] | ||
[[Category: Zhou, Y.]] | [[Category: Zhou, Y.]] | ||
| - | [[Category: SCN]] | ||
[[Category: alph-beta sandwich]] | [[Category: alph-beta sandwich]] | ||
[[Category: dna-binding protein]] | [[Category: dna-binding protein]] | ||
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[[Category: winged-helix]] | [[Category: winged-helix]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:48:22 2008'' |
Revision as of 18:48, 30 March 2008
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| , resolution 1.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | DRRD (Thermotoga maritima) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure at 1.50 A of an OmpR/PhoB Homolog from Thermotoga maritima
Overview
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.
About this Structure
1KGS is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.
Reference
Evidence of intradomain and interdomain flexibility in an OmpR/PhoB homolog from Thermotoga maritima., Buckler DR, Zhou Y, Stock AM, Structure. 2002 Feb;10(2):153-64. PMID:11839301
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