4iga
From Proteopedia
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- | + | ==The crystal structure of an activated Thermotoga maritima CheY with N-terminal region of FliM== | |
- | + | <StructureSection load='4iga' size='340' side='right' caption='[[4iga]], [[Resolution|resolution]] 1.73Å' scene=''> | |
- | + | == Structural highlights == | |
+ | <table><tr><td colspan='2'>[[4iga]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima_msb8 Thermotoga maritima msb8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IGA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IGA FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cheY, TM_0700 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 Thermotoga maritima MSB8])</td></tr> | ||
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4iga FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4iga OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4iga RCSB], [http://www.ebi.ac.uk/pdbsum/4iga PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | In bacterial chemotaxis, the levels of phosphorylated CheY in association with FliM determine the sense of the flagella rotation, which in turn controls the bacterial swimming behavior. We report the 1.7A resolution crystallographic structure of the Thermotoga maritima BeF(3)(-)-activated CheY in complex with the CheY-binding N-terminal region of FliM. Analysis of the structure in comparison to the previously reported Escherichia coli counterpart reveals that similar regions of H4-beta5-H5 in CheY and the helix in FliM are used for the complex interfaces. Our structure also indicates that the correlated movement of Phe101 and Ser82 (F-S coupling) in T. maritima CheY upon phosphorylation and FliM binding, parallels that of Tyr106 and Thr87 (Y-T coupling) demonstrated in E. coli CheY. Furthermore, significant displacements of the beta4-H4 loop in both CheYs impose a crucial role of this loop, which can be related to flagellar switch component binding or to propagating changes that is necessary during the CheY-mediated reversal of the motor. | ||
- | + | The crystal structure of an activated Thermotoga maritima CheY with N-terminal region of FliM.,Ahn DR, Song H, Kim J, Lee S, Park S Int J Biol Macromol. 2013 Mar;54:76-83. doi: 10.1016/j.ijbiomac.2012.12.003. Epub, 2012 Dec 10. PMID:23237794<ref>PMID:23237794</ref> | |
- | + | ||
- | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
- | [[ | + | </div> |
+ | |||
+ | ==See Also== | ||
+ | *[[Chemotaxis protein|Chemotaxis protein]] | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
[[Category: Thermotoga maritima msb8]] | [[Category: Thermotoga maritima msb8]] | ||
[[Category: Ahn, D R]] | [[Category: Ahn, D R]] | ||
- | [[Category: Park, S Y | + | [[Category: Park, S Y]] |
[[Category: Flim and chea]] | [[Category: Flim and chea]] | ||
[[Category: Response regulator]] | [[Category: Response regulator]] | ||
[[Category: Signaling protein-motor protein complex]] | [[Category: Signaling protein-motor protein complex]] |
Revision as of 12:19, 21 December 2014
The crystal structure of an activated Thermotoga maritima CheY with N-terminal region of FliM
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