Response regulator
From Proteopedia
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'''Response regulators''' (RR) are part of the two-component signal transduction systems which enable bacteria to sense and respond to a wide range of environments. | '''Response regulators''' (RR) are part of the two-component signal transduction systems which enable bacteria to sense and respond to a wide range of environments. | ||
- | Two-component RR is a complex of histidine kinase (sensor protein SP) and RR. The RR act as phosphorylation-activated switches. Most RR consist of N terminal shich is the signal receiving domain and C terminal which is the DNA-binding domain. For details on response regulator PleD see [[PleD activation]], [[PleD allosteric product inhibition]], [[PleD catalysis]]. | + | Two-component RR is a complex of histidine kinase (sensor protein SP) and RR. The RR act as phosphorylation-activated switches. Most RR consist of N terminal shich is the signal receiving domain and C terminal which is the DNA-binding domain. For details on response regulator PleD see [[PleD activation]], [[PleD allosteric product inhibition]], [[PleD catalysis]]. For details on PhoP see [[PhoP Regulatory Domain]] and [[PhoP-PhoQ]]. |
Revision as of 09:29, 18 August 2011
Response regulators (RR) are part of the two-component signal transduction systems which enable bacteria to sense and respond to a wide range of environments. Two-component RR is a complex of histidine kinase (sensor protein SP) and RR. The RR act as phosphorylation-activated switches. Most RR consist of N terminal shich is the signal receiving domain and C terminal which is the DNA-binding domain. For details on response regulator PleD see PleD activation, PleD allosteric product inhibition, PleD catalysis. For details on PhoP see PhoP Regulatory Domain and PhoP-PhoQ.
Contents |
3D Structures of response regulator
3sft – TmCheB methyltransferase catalytic domain – Thermotoga maritima
1p2f – TmDrrB
3gl9, 3dgf – TmRR
3snk – CheY-like – Mesorhizobium loti
3crn, 3cg4 - CheY-like – Methanospirillum hungatei
1ixm – BsSpo0B
1nat – BsSPo0F
1srr - BsSPo0F (mutant)
3p3q – McMmoQ (mutant) – Methylococcus capsulatus
3ljx – McMmoQ residues 20-298
3n0r – CvPhyR – Caulobacter vibrioides
1m5t, 1m5u - CvDivK
3n53 – RR – Pelobacter carbinolicus
3nhm – MxRR – Myxococcus xanthus
3kto - RR – Pseudoalteromonas atlantica
3f7a, 3eq2 – PaRssB – Pseudomonas aeruginosa
3es2 – PaRssB phosphatase domain
3i5b – PaWpsR GGDEF domain
3i5c - PaWpsR GGDEF domain/GCN4 leucine zipper
1yio, 1zn2 – PfStyR – Pseudomonas fluorescens
3hdv – RR – Pseudomonas putida
3i5a – WpsR – Pseudomonas syringae
3heb – CheY – Rhodospirillum rubrum
3eqz – CpRR – Colwellia psychrerythraea
2zay – RR residues 150-285 – Desulfuromonas acetoxidans
2rdm – RR (mutant) – Sinorhizobium medicae
1xhe – EcArcA (mutant) - Escherichia coli
1jbe - EcCheY
1nxo, 1nxp, 1nxs, 1nxt, 1nxv, 1nxw, 1nxx – SpRR MICA receiver domain
2gwr – MtMtrA - Mycobacterium tuberculosis
1ys6 – MtPrrA
1k66 – ToRcpB – Tolypothrix
1k68 – ToRcpA
3p01 – RR residues 134-315 – Nostoc
3ilh – RR – Cytophaga hutchinsonii
3c3w – MtDosR
2qvg – RR – Legionella pneumophila
2qr3 – RR – Bacterioides fragilis
Response regulator signal receiving domain
2qxy – TmRR
3i42 - CheY-like – Methylobacillus flagellatus
2zwm– BsYycF
1mvo - BsPhoP
3gkg, 2i6f – MxFrzS
2nt3, 2nt4 - MxFrzS (mutant)
3lte – RR – Bermanella marisrubri
3hv2 – PfRR
3kht – RR – Hahella chejuensis
3jte – CtRR - Clostridium thermocellum
3cnb – CpRR
3c3m – RR – Methanoculleus marisnigri
2qsj – LuxR – Silicibacter pomeroyi
2pln – RR – Helicobacter pylori
2jb9, 2jba – EcPhoB (mutant)
3lua – CtRR
3lsg – YesN – Fusobacterium nucleatum
3cz5 – LuxR – Aurantimonas
2qzj – RR – Clostridium difficile
1a04, 1rnl – EcNarL
Response regulator DNA-binding domain
2zxj - SaYycF - Staphylococcus aureus
2rnj - SaVraR - NMR
2hwv – VicR – Enterococcus faecalis
1umq – PrrA – Rhodobacter sphaeroides – NMR
3c57 – MtDosR
2pmu – MtPhoP
Response regulator complex
3nnn – TmDrrD signal receiving domain + BeF3
3nns – TmDrrB signal receiving domain + BeF3
3a0u - TmTrrA + Mg + BeF3
3a10 - TmTrrA (mutant) + Mg + BeF3
3rqi – RR + phosphorylated aspartic acid + citrate + Ca – Burkholderia pseudomallei
3q15 – BsRapH + sporulation initiation phosphotransferase – Bacillus subtilis
3m6m – RpfF residues 400-541 + RpfF protein REC domain – Xanthomonas campestris
1mav, 1mb0, 1mb3 – CvDivK + metal ion
2wb4 – PleD + cyclic diguanosine monophosphate + BeF3 – Caulobacter crescentus
2v0n – CvPleD residues 2-454 + cyclic diguanosine monophosphate + GTP + BeF3
3hzh – CheX + CheY + Mg + BeF3 – Borrelia burgdorferi
1xhf - EcArcA (mutant) + BeF3
2a9o, 2a9p, 2a9q, 2a9r – SpYycF + BeF3 – Streptococcus pneumoniae
1ys7 – MtPrrA + Mg
1jlk, 1i3c – Rcp1 + Mn]] - Synechocystis
3dge – TmRR + SP cytoplasmic domain
3a0r – TmTrrA + histidine kinase ThkA
1zg1, 1zg5, 1je8 – EcNarL DNA-binding domain + DNA
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Michal Harel, Joel L. Sussman, Alexander Berchansky, Jaime Prilusky