3a7m: Difference between revisions

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==Structure of FliT, the flagellar type III chaperone for FliD==
==Structure of FliT, the flagellar type III chaperone for FliD==
<StructureSection load='3a7m' size='340' side='right' caption='[[3a7m]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
<StructureSection load='3a7m' size='340' side='right'caption='[[3a7m]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3a7m]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_typhimurium"_loeffler_1892 "bacillus typhimurium" loeffler 1892]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A7M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3A7M FirstGlance]. <br>
<table><tr><td colspan='2'>[[3a7m]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_typhimurium"_loeffler_1892 "bacillus typhimurium" loeffler 1892]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A7M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A7M FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fliT, STM1962 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 "Bacillus typhimurium" Loeffler 1892])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fliT, STM1962 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 "Bacillus typhimurium" Loeffler 1892])</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=3a7m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a7m OCA], [http://pdbe.org/3a7m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3a7m RCSB], [http://www.ebi.ac.uk/pdbsum/3a7m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3a7m ProSAT]</span></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=3a7m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a7m OCA], [https://pdbe.org/3a7m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a7m RCSB], [https://www.ebi.ac.uk/pdbsum/3a7m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a7m ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/FLIT_SALTY FLIT_SALTY]] Dual-function protein that regulates the transcription of class 2 flagellar operons and that also acts as an export chaperone for the filament-capping protein FliD. As a transcriptional regulator, acts as an anti-FlhDC factor; it directly binds FlhC, thus inhibiting the binding of the FlhC/FlhD complex to class 2 promoters, resulting in decreased expression of class 2 flagellar operons. As a chaperone, effects FliD transition to the membrane by preventing its premature polymerization, and by directing it to the export apparatus.<ref>PMID:10320579</ref> <ref>PMID:10791024</ref> <ref>PMID:11169117</ref> <ref>PMID:16952964</ref>   
[[https://www.uniprot.org/uniprot/FLIT_SALTY FLIT_SALTY]] Dual-function protein that regulates the transcription of class 2 flagellar operons and that also acts as an export chaperone for the filament-capping protein FliD. As a transcriptional regulator, acts as an anti-FlhDC factor; it directly binds FlhC, thus inhibiting the binding of the FlhC/FlhD complex to class 2 promoters, resulting in decreased expression of class 2 flagellar operons. As a chaperone, effects FliD transition to the membrane by preventing its premature polymerization, and by directing it to the export apparatus.<ref>PMID:10320579</ref> <ref>PMID:10791024</ref> <ref>PMID:11169117</ref> <ref>PMID:16952964</ref>   
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</div>
</div>
<div class="pdbe-citations 3a7m" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 3a7m" style="background-color:#fffaf0;"></div>
==See Also==
*[[Flagellar protein 3D structures|Flagellar protein 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Bacillus typhimurium loeffler 1892]]
[[Category: Bacillus typhimurium loeffler 1892]]
[[Category: Large Structures]]
[[Category: Imada, K]]
[[Category: Imada, K]]
[[Category: Kinoshita, M]]
[[Category: Kinoshita, M]]