2hp7: Difference between revisions

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-[[Image:2hp7.gif|left|200px]]
-<!--
+==Structure of FliM provides insight into assembly of the switch complex in the bacterial flagella motor==
-The line below this paragraph, containing "STRUCTURE_2hp7", creates the "Structure Box" on the page.
+<StructureSection load='2hp7' size='340' side='right'caption='[[2hp7]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2hp7]] is a 1 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=2HP7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HP7 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</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&#8491;</td></tr>
--->
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2hp7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hp7 OCA], [https://pdbe.org/2hp7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hp7 RCSB], [https://www.ebi.ac.uk/pdbsum/2hp7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hp7 ProSAT]</span></td></tr>
-{{STRUCTURE_2hp7|  PDB=2hp7  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/FLIM_THEMA FLIM_THEMA] FliM is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheX chemotaxis proteins, 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/hp/2hp7_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=2hp7 ConSurf].
+<div style="clear:both"></div>
-'''Structure of FliM provides insight into assembly of the switch complex in the bacterial flagella motor'''
+==See Also==
+*[[Flagellar protein 3D structures|Flagellar protein 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-Bacteria switch the direction their flagella rotate to control movement. FliM, along with FliN and FliG, compose a complex in the motor that, upon binding phosphorylated CheY, reverses the sense of flagellar rotation. The 2.0-A resolution structure of the FliM middle domain (FliM(M)) from Thermotoga maritima reveals a pseudo-2-fold symmetric topology similar to the CheY phosphatases CheC and CheX. A variable structural element, which, in CheC, mediates binding to CheD (alpha2') and, in CheX, mediates dimerization (beta'(x)), has a truncated structure unique to FliM (alpha2'). An exposed helix of FliM(M) (alpha1) does not contain the catalytic residues of CheC and CheX but does include positions conserved in FliM sequences. Cross-linking experiments with site-directed cysteine mutants show that FliM self-associates through residues on alpha1 and alpha2'. CheY activated by BeF(3)(-) binds to FliM with approximately 40-fold higher affinity than CheY (K(d) = 0.04 microM vs. 2 microM). Mapping residue conservation, suppressor mutation sites, binding data, and deletion analysis onto the FliM(M) surface defines regions important for contacts with the stator-interacting protein FliG and for either counterclockwise or clockwise rotation. Association of 33-35 FliM subunits would generate a 44- to 45-nm-diameter disk, consistent with the known dimensions of the C-ring. The localization of counterclockwise- and clockwise-biasing mutations to distinct surfaces suggests that the binding of phosphorylated CheY cooperatively realigns FliM around the ring.
+[[Category: Large Structures]]
-==About this Structure==
-HP7 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=2HP7 OCA].
-==Reference==
-Structure of FliM provides insight into assembly of the switch complex in the bacterial flagella motor., Park SY, Lowder B, Bilwes AM, Blair DF, Crane BR, Proc Natl Acad Sci U S A. 2006 Aug 8;103(32):11886-91. Epub 2006 Aug 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16882724 16882724]
-[[Category: Single protein]]
 [[Category: Thermotoga maritima]]
-[[Category: Bilwes, A M.]]
+[[Category: Bilwes AM]]
-[[Category: Blair, D F.]]
+[[Category: Blair DF]]
-[[Category: Crane, B R.]]
+[[Category: Crane BR]]
-[[Category: Lowder, B.]]
+[[Category: Lowder B]]
-[[Category: Park, S.]]
+[[Category: Park S]]
-[[Category: Bacterial chemotaxis]]
-[[Category: Flagellar switch complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 06:32:25 2008''