Chemotaxis protein: Difference between revisions

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<StructureSection load='1e6m' size='350' side='right' caption='E. coli CheY (PDB entry [[1e6m]])' scene=''>
<StructureSection load='1e6m' size='350' side='right' caption='E. coli CheY (PDB entry [[1e6m]])' scene=''>


'''Chemotaxis proteins''' direct cell movement according to certain chemicals in their environment.
'''Chemotaxis proteins''' direct cell movement according to certain chemicals in their environment.<ref>PMID:4598187</ref>
For details on '''chemotaxis protein''' see<br />
*'''CheY''' is a response regulator determining the swimming behaviour of the cell<ref>PMID:7623663</ref>.
*[[Molecular Playground/Bacterial Chemotaxis Receptors]] for CheW<br />
*'''CheR''' is a SAM-dependent methyltransferase which binds to the C-terminus of some chemotaxis receptors and methylates neighbouring receptor molecules<ref>PMID:9628482</ref>.  See [[Molecular Playground/CheR]] and [[Chemotaxis receptor methyltransferase]].
*[[Molecular Playground/Bacterial Chemotaxis Complex]] for CheA and CheW<br />
*'''CheA''' is a histidine kinase which donates phosphoric groups to CheB and CheY to control swimming behaviour<ref>PMID:15090507</ref>.  See [[Molecular Playground/CheA]].
*[[Molecular Playground/CheA]] for CheA<br />
*'''CheB''' is a methyltransferase catalysing the demethylationof chemotaxis membrane receptors in ''Salmonella typhimurium''<ref>PMID:2991277</ref>.
*[[Molecular Playground/CLOCK:BMAL1 heterodimer complex]]<br />
*'''CheW''' participates in the control of CheA activity<ref>PMID:1992467</ref>. See [[Molecular Playground/Bacterial Chemotaxis Receptors]]  
*[[Molecular Playground/Cytoplasmic domain of chemoreceptor of Thermotoga maritima]]<br />
*'''PomA''' and '''PomB''' convert Na+ flux through channel to rotation of the flagellum in several bacteria <ref>PMID:21642461</ref>.
*[[Receiver domain of sensor histidine kinase CKI1]].
*'''Aspartate chemotaxis receptor''' or '''Tar''' modulates the activity of CheA<ref>PMID:8832891</ref>. See [[DNA Origami Assembly for the Tar Chemoreceptor]].
</StructureSection>
*'''Methyl-accepting chemotaxis protein''' are the predominant chemoreceptors in bacteria and archaea.  They are involved in regulation of diverse aspects of cellular activities<ref>PMID:28409190</ref>.  See [[Molecular Playground/cytoplasmic domain of a serine chemotaxis receptor]].
==3D structures of chemotaxis protein ==
*'''FLiN''', '''MotA''' and '''MotB''' are involved in energizing flagellar rotation in ''E. coli''<ref>PMID:7892209</ref>.
*'''CKI1''' is a histidine kinase involved in cytokinin signal transduction<ref>PMID:8875940</ref>. See [[Receiver domain of sensor histidine kinase CKI1]].


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
See also:
{{#tree:id=OrganizedByTopic|openlevels=0|


*CheY
*[[Molecular Playground/Cytoplasmic domain of chemoreceptor of Thermotoga maritima]]<br />


**[[1ab6]], [[1d4z]], [[1e6m]], [[1e6k]], [[1e6l]], [[1jbe]], [[1mih]], [[3oo0]], [[3oo1]] – EcCheY (mutant) – ''Escherichia coli''<BR />
==3D structures of chemotaxis protein ==
**[[1tmy]], [[2tmy]], [[3tmy]], [[4tmy]] - TmCheY – ''Thermotoga maritima''<br />
[[Chemotaxis protein 3D structures]]
**[[4h60]], [[4hnr]], [[4jp1]] – VcCheY – ''Vibrio cholerae''<br />
**[[4hnq]] - VcCheY (mutant) <br />
**[[3gwg]] – HpCheY -  ''Helicobacter pylori''<BR />
**[[3h1f]], [[3h1g]] - HpCheY (mutant) <BR />
**[[2id7]], [[2id9]], [[2idm]] – EcCheY-phosphono (mutant) <BR />
**[[1djm]] – EcCheY – NMR<BR />
**[[2chy]] – StCheY - ''Salmonella typhimurium'' <br />


*''CheY complexes''
</StructureSection>
 
**[[1zdm]] – EcCheY + Xe<BR />
**[[3h1e]] - HpCheY  + BeF3 + Mn<BR />
**[[3f7n]], [[3fft]], [[3ffw]], [[3ffx]], [[3fgz]], [[3myy]], [[3olv]], [[3olw]], [[3olx]], [[3oly]] - EcCheY (mutant) + BeF3 + Mn<BR />
**[[4hns]] - VcCheY + BeF3 + Mg<br />
**[[4lx8]] - VcCheY + Mg<br />
**[[1fqw]] - EcCheY  + BeF3 + Mn<br />
**[[3rvj]], [[3rvk]], [[3rvl]], [[3rvm]], [[3rvn]], [[3rvo]], [[3rvp]], [[3rvq]], [[3rvr]], [[3rvs]] - EcCheY (mutant) + BeF3 + Mn<br />
**[[1bdj]] – EcCheY + aerobic respiration control protein HPT domain<BR />
**[[1u8t]] – EcCheY + flagellar motor switch protein FLIM<BR />
**[[2b1j]], [[1f4v]] - EcCheY + flagellar motor switch protein FLIM N terminal<br />
**[[1ffg]], [[1ffs]] – EcCheY + CheA CheY-binding domain<BR />
**[[1u0s]] - TmCheY response regulating domain + CheA P2 domain <BR />
**[[1ffw]] – EcCheY + CheA CheY-binding domain + imido phosphate<BR />
**[[1kmi]] - EcCheY + CheZ<BR />
**[[2lp4]] - EcCheY + CheA<br />
**[[2fka]], [[2flk]], [[2flw]], [[2fmf]], [[2fmh]], [[2fmi]], [[2fmk]], [[2pl9]], [[2pmc]] – StCheY + CheZ  peptide <BR />
**[[2che]], [[2chf]] – StCheY + Mg<br />
**[[4iga]] - TmCheY + flagellar motor switch protein FLIM peptide<br />
 
*CheX
 
**[[1xko]]– TmCheX<BR />
**[[3hm4]] – CheX – ''Desulfovibrio desulfuricans''<BR />
**[[3hzh]] – CheX + Che-3 – ''Borrelia burgdorferi''<br />
 
*CheC
 
**[[1xkr]] – TmCheC<BR />
**[[2f9z]] – TmCheC + CheD<BR />
**[[3qta]] – CheC – ''Haloarcula marismortui''<BR />
 
*CheR
 
**[[1bc5]] – StCheR + chemotaxis receptor peptide <BR />
**[[1af7]] – StCheR<br />
 
*CheA
 
**[[1fwp]] – EcCheA – NMR<br />
**[[1b3q]] – TmCheA dimerization, kinase and regulatory domains <BR />
**[[1i5n]] – StCheA P1 domain<br />
**[[1i58]], [[1i59]], [[1i5a]], [[1i5b]], [[1i5d]] - TmCheA P4 domain + ATP analog<br />
**[[1i5c]] - TmCheA P4 domain (mutant) + ADP<br />
**[[1tqg]] – TmCheA phosphotransferase domain<br />
**[[2ld6]] – TmCheA HPT domain - NMR<BR />
**[[2ch4]] - TmCheA kinase and regulatory domains + CheW<br />
**[[3ur1]], [[4jpb]] – TmCheA + CheW + methyl-accepting Che<br />
 
*CheB
 
**[[1a2o]], [[1chd]]– StCheB<br />
 
*CheW
 
**[[1k0s]] – TmCheW<br />
**[[2ho9]] – EcCheW - NMR<BR />
 
*Aspartate chemotaxis receptor
 
**[[1jmw]], [[1vls]] – StChe LBD<br />
**[[1lih]] – StChe LBD (mutant)<br />
**[[1was]] – StChe LBD<br />
**[[1wat]], [[1vlt]], [[2lig]] – StChe LBD + aspartate<br />
**[[2asr]] – EcChe <br />
 
*Methyl-accepting chemotaxis protein
 
**[[2m7u]], [[2m7v]] – TeMche – ''Thermosynechococcus elongatus''<br />
**[[3vv4]] – TeMche GAF domain<br />
**[[4fof]], [[4glq]] – TeMche GAF domain (mutant)<br />
**[[3w2z]] – Mche residues 221-397 – Nostoc<br />
**[[3g67]] – TmMche<BR />
**[[3g6b]] – TmMche (mutant) <BR />
**[[2ch7]] – TmMche cytoplasmic domain<BR />
**[[1qu7]] – EcMcheI cytoplasmic domain<BR />
**[[2ld6]] – EcMche peptide - NMR<BR />
**[[3atp]] -  EcMcheI LBD + serine<BR />
**[[2d4u]] – EcMcheI LBD (mutant)<br />
**[[3zx6]] – EcMcheI/HAMP<br />
**[[1jmw]] - StMche LBD (mutant) <BR />
**[[2qhk]], [[4exo]] – Mche N-terminal – ''Vibrio parahaemolyticus''<BR />
**[[3c8c]] – Mche N-terminal <BR />
**[[3b47]] – Mche periplasmic domain – ''Geobacter sulfurreducens''<BR />
**[[4it2]] - Mche H-Nox domain Mn-porphyrin – ''Caldanaerobacter subterraneus''<br />
 
*''Heme-containing methyl-accepting chemotaxis protein''
 
**[[3eee]], [[3iqb]], [[3lah]], [[3lai]], [[3sj5]], [[4fdk]] – TtMche H-Nox domain (mutant)<br />
**[[1xbn]] – TtMche – Thermoanaerobacter tengcongensis<br />
**[[1u4h]], [[1u55]], [[1u56]], [[3tf0]], [[3tf1]] - TtMche H-Nox domain<br />
**[[3m0b]] - TtMche H-Nox domain Ru-porphyrin<br />
**[[3nvr]], [[3nvu]] – TtMche N terminal (mutant)<br />
 
*Flagellar motor protein FLIN
 
**[[1yab]] – TmFLIN<BR />
 
*Chemotaxis protein MotB


**[[3cyp]], [[3imp]], [[3s02]], [[3s03]], [[3s06]], [[3s0h]], [[3s0w]], [[3s0y]] – HpMotB C terminal<br />
== References ==
**[[3cyq]] – HpMotB C terminal + N-acetylmuramic acid<BR />
<references/>
**[[2zov]], [[2zvy]], [[2zvz]] - StMotB C terminal<br />
}}
[[Category:Topic Page]]
[[Category:Topic Page]]

Latest revision as of 11:28, 27 January 2025


Chemotaxis proteins direct cell movement according to certain chemicals in their environment.[1]

See also:

3D structures of chemotaxis protein

Chemotaxis protein 3D structures


E. coli CheY (PDB entry 1e6m)

Drag the structure with the mouse to rotate

ReferencesReferences

  1. ↑ Adler J, Tso WW. "Decision"-making in bacteria: chemotactic response of Escherichia coli to conflicting stimuli. Science. 1974 Jun 21;184(4143):1292-4. PMID:4598187
  2. ↑ Sanna MG, Swanson RV, Bourret RB, Simon MI. Mutations in the chemotactic response regulator, CheY, that confer resistance to the phosphatase activity of CheZ. Mol Microbiol. 1995 Mar;15(6):1069-79. PMID:7623663 doi:10.1111/j.1365-2958.1995.tb02282.x
  3. ↑ Djordjevic S, Stock AM. Chemotaxis receptor recognition by protein methyltransferase CheR. Nat Struct Biol. 1998 Jun;5(6):446-50. PMID:9628482
  4. ↑ Jahreis K, Morrison TB, Garzón A, Parkinson JS. Chemotactic signaling by an Escherichia coli CheA mutant that lacks the binding domain for phosphoacceptor partners. J Bacteriol. 2004 May;186(9):2664-72. PMID:15090507 doi:10.1128/JB.186.9.2664-2672.2004
  5. ↑ Simms SA, Keane MG, Stock J. Multiple forms of the CheB methylesterase in bacterial chemosensing. J Biol Chem. 1985 Aug 25;260(18):10161-8. PMID:2991277
  6. ↑ Gegner JA, Dahlquist FW. Signal transduction in bacteria: CheW forms a reversible complex with the protein kinase CheA. Proc Natl Acad Sci U S A. 1991 Feb 1;88(3):750-4. PMID:1992467 doi:10.1073/pnas.88.3.750
  7. ↑ Yonekura K, Maki-Yonekura S, Homma M. Structure of the flagellar motor protein complex PomAB: implications for the torque-generating conformation. J Bacteriol. 2011 Aug;193(15):3863-70. PMID:21642461 doi:10.1128/JB.05021-11
  8. ↑ Tatsuno I, Homma M, Oosawa K, Kawagishi I. Signaling by the Escherichia coli aspartate chemoreceptor Tar with a single cytoplasmic domain per dimer. Science. 1996 Oct 18;274(5286):423-5. PMID:8832891 doi:10.1126/science.274.5286.423
  9. ↑ Salah Ud-Din AIM, Roujeinikova A. Methyl-accepting chemotaxis proteins: a core sensing element in prokaryotes and archaea. Cell Mol Life Sci. 2017 Sep;74(18):3293-3303. PMID:28409190 doi:10.1007/s00018-017-2514-0
  10. ↑ Garza AG, Harris-Haller LW, Stoebner RA, Manson MD. Motility protein interactions in the bacterial flagellar motor. Proc Natl Acad Sci U S A. 1995 Mar 14;92(6):1970-4. PMID:7892209 doi:10.1073/pnas.92.6.1970
  11. ↑ Kakimoto T. CKI1, a histidine kinase homolog implicated in cytokinin signal transduction. Science. 1996 Nov 8;274(5289):982-5. PMID:8875940

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