Response regulator

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Template:STRUCTURE 1zg1

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. RR CheY is a chemotaxis response regulator in bacteria. RR Spo0 is the sporulation response regulator. 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.


3D Structures of response regulator

Updated December 2011

Nitrate/nitrite RR

1rnl, 1a04 – EcNarL – Escherichia coli
1je8, 1zg1, 1zg5 – EcNarL DNA-binding domain + DNA

Sporulation RR

1srr – BsSpo0F (mutant) – Bacillus subtilis
1nat - BsSpo0F
3q15 - BsSpo0F + RR aspartate phosphatase
1ixm - BsSpo0B
1fc3 – Spo0A trans-activation domain – Geobacillus stearothermophilus

DNA-binding RR

1kgs – TmDrrD – Thermotoga maritima
3nnn – TmDrrD receiver domain + BeF3
1p2f – TmDrrB
3nns - TmDrrB receiver domain + BeF3
1nxo, 1nxp, 1nxs, 1nxt, 1nxv, 1nxw, 1nxx – SpMicArec receiver domain – Streptococcus pneumonia
2gwr - MtMtrA – Mycobacterium tuberculosis
2hwv – VicR C terminal – Enterococcus faecalis
2qsj – LuxR – Silicibbacter pomeroyi
3cnb, 3eqz]] – MerR receiver domain – Colwellia psychrerythraea
2rnj – SaVraR DNA-binding domain – Staphylococcus aureus – NMR
2zxj - SaWalR DNA-binding domain
3q9s – DrRR receiver domain – Deinococcus radiodurans
3q9v - DrRR C terminal


Cyanobacterial phytochrome RR

1i3c – SyRcp1 – Synechocystis
1jlk – SyRcp1 + Mn
1k66 – ToRcpB – Tolypothrix
1k68 – ToRcpB

Phosphatase synthesis RR

1mvo – BsPhoP receiver domain
2jb9, 2jba – EcPhoB (mutant)
2pmu – MtPhoP DNA-binding domain

Polar differentiation RR

1m5t, 1m5u – CvDivK – Caulobacter vibrioides
1mav, 1mb0, 1mb3 – CvDivK + cation

Photosynthetic apparatus RR

1umq – PrrA DNA-binding domain – Rhodobacter sphaeroides – NMR
1ys6 – MtPrrA
1ys7 – MtPrrA + Mg

Redox RR

1xhe – EcArcA receiver domain
1xhf – EcArcA receiver domain + BeF3

Social motility RR

2gkg, 2i6f – MxFrzS receiver domain – Myxococcus xanthus
2nt3, 2nt4 - MxFrzS receiver domain (mutant)

Stalked-cell differentiation RR

2v0n – CvPleD + GMP + GTP
2wb4, 1w25]] - CvPleD + GMP

Hypoxic RR

3c3w – MtDosR
3c57 – MtDosR C terminal

Transcriptional RR

2zwm – BsYycF receiver domain
3ulq – BsComA DNA-binding domain + RR aspartate phosphatase

Stress RR

3n0r – CVPhyR

CheY-like RR

3snk – RR – Mesorhizobium loti
3cg4, 3crn - RR receiver domain – Methanospirillum hungatei
3i42 – RR receiver domain – Methylobacter flagellates

Unspecified RR receiver domain

2a9o, 2a9p, 2a9q – SpRR + Mn + BeF3
2a9r – SpRR + phosphate + Mg
2pln – HP1043 – Helicobacter pylori
2qr3 – RR – Bacteroides fragilis
2qxy – TmRR
2qzj – RR – Clostridium difficile
3kht – RR – Hahella chejuensis
3c3m – RR – Methanoculleus marisnigri
3cz5 – RR – Aurantimonas
3heb - RR – Rhodospirillum rubrum
3lte – RR – Bermanella marisrubri
3jte, 3lua – RR – Clostridium thermocellum

Unspecified RR

1yio, 1zn2 – StyR – Pseudomonas fluorescens
3a0u, 3a10 – TmTrrA + Mg + BeF3
2qvg – RR – Legionella pneumophila
3gl9 - TmRR
2zay – RR – Desulfuromonas acetoxidans
2rdm – RR (mutant) – Sinorhizobium medicae
3bre – PaRR – Pseudomonas aeruginosa
3hdv – RR – Pseudomonas putida
3i5a – PsWspR – Pseudomonas syringae
3ilh – RR – Cytophaga hutchinsonii
3i5b – PaWspR GGDEF domain
3i5c – PaWspR GGDEF domain/GCN4 leucine zipper
3ljx – McMmoQ – Methylococcus capsulatus
3p3q – McMmoQ (mutant)
3lsg – RR C terminal – Fusobacterium nucleatum
3nhm – MxRR
3m6m – XcRpfC REC domain + enoyl-CoA hydratase – Xanthomonas campestris
3qyy – XcRR GGDEF domain + GMP
3p01 – RR residues 134-315 – Nostoc
3rqi – RR + phosphate + Ca + citrate – Burkholderia pseudomallei
3kto – RR - Pseudoalteromonas atlantica

RR complex with histidine kinase

3dge, 3dgf]] – TmRR + sensor protein
3a0r – TmTrrA (mutant) + sensor protein

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Joel L. Sussman, Alexander Berchansky, Jaime Prilusky

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