1qc7: Difference between revisions

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[[Image:1qc7.jpg|left|200px]]


{{Structure
==T. MARITIMA FLIG C-TERMINAL DOMAIN==
|PDB= 1qc7 |SIZE=350|CAPTION= <scene name='initialview01'>1qc7</scene>, resolution 2.2&Aring;
<StructureSection load='1qc7' size='340' side='right'caption='[[1qc7]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1qc7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QC7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QC7 FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
|GENE= FLIG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima])
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qc7 OCA], [https://pdbe.org/1qc7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qc7 RCSB], [https://www.ebi.ac.uk/pdbsum/1qc7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qc7 ProSAT]</span></td></tr>
|DOMAIN=
</table>
|RELATEDENTRY=
== Function ==
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qc7 OCA], [http://www.ebi.ac.uk/pdbsum/1qc7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qc7 RCSB]</span>
[https://www.uniprot.org/uniprot/FLIG_THEMA FLIG_THEMA] One of the proteins that forms a switch complex that is proposed to be located at the base of the basal body. This complex interacts with chemotaxis proteins (such as CheY) in addition to contacting components of the motor that determine the direction of flagellar rotation (By similarity).
}}
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qc/1qc7_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qc7 ConSurf].
<div style="clear:both"></div>


'''T. MARITIMA FLIG C-TERMINAL DOMAIN'''
==See Also==
 
*[[Flagellar protein 3D structures|Flagellar protein 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
Many motile species of bacteria are propelled by flagella, which are rigid helical filaments turned by rotary motors in the cell membrane. The motors are powered by the transmembrane gradient of protons or sodium ions. Although bacterial flagella contain many proteins, only three-MotA, MotB and FliG-participate closely in torque generation. MotA and MotB are ion-conducting membrane proteins that form the stator of the motor. FliG is a component of the rotor, present in about 25 copies per flagellum. It is composed of an amino-terminal domain that functions in flagellar assembly and a carboxy-terminal domain (FliG-C) that functions specifically in motor rotation. Here we report the crystal structure of FliG-C from the hyperthermophilic eubacterium Thermotoga maritima. Charged residues that are important for function, and which interact with the stator protein MotA, cluster along a prominent ridge on FliG-C. On the basis of the disposition of these residues, we present a hypothesis for the orientation of FliG-C domains in the flagellar motor, and propose a structural model for the part of the rotor that interacts with the stator.
[[Category: Large Structures]]
 
==About this Structure==
1QC7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QC7 OCA].
 
==Reference==
Structure of the C-terminal domain of FliG, a component of the rotor in the bacterial flagellar motor., Lloyd SA, Whitby FG, Blair DF, Hill CP, Nature. 1999 Jul 29;400(6743):472-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10440379 10440379]
[[Category: Single protein]]
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
[[Category: Blair, D.]]
[[Category: Blair D]]
[[Category: Hill, C P.]]
[[Category: Hill CP]]
[[Category: Lloyd, S A.]]
[[Category: Lloyd SA]]
[[Category: Whitby, F G.]]
[[Category: Whitby FG]]
[[Category: flagellar motor switch protein]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:11:49 2008''

Latest revision as of 11:14, 14 February 2024

T. MARITIMA FLIG C-TERMINAL DOMAINT. MARITIMA FLIG C-TERMINAL DOMAIN

Structural highlights

1qc7 is a 2 chain structure with sequence from Thermotoga maritima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FLIG_THEMA One of the proteins that forms a switch complex that is proposed to be located at the base of the basal body. This complex interacts with chemotaxis proteins (such as CheY) in addition to contacting components of the motor that determine the direction of flagellar rotation (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1qc7, resolution 2.20Å

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