1ucu
From Proteopedia
(Difference between revisions)
Line 3: | Line 3: | ||
<SX load='1ucu' size='340' side='right' viewer='molstar' caption='[[1ucu]], [[Resolution|resolution]] 4.00Å' scene=''> | <SX load='1ucu' size='340' side='right' viewer='molstar' caption='[[1ucu]], [[Resolution|resolution]] 4.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1ucu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1ucu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UCU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UCU FirstGlance]. <br> |
- | </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=1ucu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ucu OCA], [https://pdbe.org/1ucu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ucu RCSB], [https://www.ebi.ac.uk/pdbsum/1ucu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ucu ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4Å</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=1ucu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ucu OCA], [https://pdbe.org/1ucu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ucu RCSB], [https://www.ebi.ac.uk/pdbsum/1ucu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ucu ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
- | + | [https://www.uniprot.org/uniprot/FLIC_SALTY FLIC_SALTY] Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Line 18: | Line 19: | ||
</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=1ucu ConSurf]. | </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=1ucu ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | The bacterial flagellar filament is a helical propeller for bacterial locomotion. It is a helical assembly of a single protein, flagellin, and its tubular structure is formed by 11 protofilaments in two distinct conformations, L- and R-type, for supercoiling. The X-ray crystal structure of a flagellin fragment lacking about 100 terminal residues revealed the protofilament structure, but the full filament structure is still essential for understanding the mechanism of supercoiling and polymerization. Here we report a complete atomic model of the R-type filament by electron cryomicroscopy. A density map obtained from image data up to 4 A resolution shows the feature of alpha-helical backbone and some large side chains. The atomic model built on the map reveals intricate molecular packing and an alpha-helical coiled coil formed by the terminal chains in the inner core of the filament, with its intersubunit hydrophobic interactions having an important role in stabilizing the filament. | ||
- | |||
- | Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy.,Yonekura K, Maki-Yonekura S, Namba K Nature. 2003 Aug 7;424(6949):643-50. PMID:12904785<ref>PMID:12904785</ref> | ||
- | |||
- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1ucu" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Flagellin 3D structures|Flagellin 3D structures]] | *[[Flagellin 3D structures|Flagellin 3D structures]] | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</SX> | </SX> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Salmonella | + | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium]] |
- | [[Category: Maki-Yonekura | + | [[Category: Maki-Yonekura S]] |
- | [[Category: Namba | + | [[Category: Namba K]] |
- | [[Category: Yonekura | + | [[Category: Yonekura K]] |
- | + | ||
- | + | ||
- | + | ||
- | + |
Current revision
R-type straight flagellar filament made of full-length flagellin
|