3b1s: Difference between revisions

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<StructureSection load='3b1s' size='340' side='right'caption='[[3b1s]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
<StructureSection load='3b1s' size='340' side='right'caption='[[3b1s]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3b1s]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/"aquifex_aeolicus"_huber_and_stetter_2001 "aquifex aeolicus" huber and stetter 2001]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B1S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3B1S FirstGlance]. <br>
<table><tr><td colspan='2'>[[3b1s]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B1S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3B1S FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3b0z|3b0z]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.55&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">flhB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=63363 "Aquifex aeolicus" Huber and Stetter 2001])</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=3b1s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b1s OCA], [https://pdbe.org/3b1s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b1s RCSB], [https://www.ebi.ac.uk/pdbsum/3b1s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b1s 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=3b1s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b1s OCA], [https://pdbe.org/3b1s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b1s RCSB], [https://www.ebi.ac.uk/pdbsum/3b1s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b1s ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/FLHB_AQUAE FLHB_AQUAE]] Required for formation of the rod structure in the basal body of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin (By similarity).  
[https://www.uniprot.org/uniprot/FLHB_AQUAE FLHB_AQUAE] Required for formation of the rod structure in the basal body of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The membrane protein FlhB is a highly conserved component of the flagellar secretion system. It is composed of an N-terminal transmembrane domain and a C-terminal cytoplasmic domain (FlhBC). Here, the crystal structures of FlhBC from Salmonella typhimurium and Aquifex aeolicus are described at 2.45 and 2.55 A resolution, respectively. These flagellar FlhBC structures are similar to those of paralogues from the needle type III secretion system, with the major difference being in a linker that connects the transmembrane and cytoplasmic domains of FlhB. It was found that deletion of a short flexible loop in a globular part of Salmonella FlhBC leads to complete inhibition of secretion by the flagellar secretion system. Molecular-dynamics calculations demonstrate that the linker region is the most flexible part of FlhBC and that the deletion of the loop reduces this flexibility. These results are in good agreement with previous studies showing the importance of the linker in the function of FlhB and provide new insight into the relationship between the different parts of the FlhBC molecule.
 
Inhibition of a type III secretion system by the deletion of a short loop in one of its membrane proteins.,Meshcheryakov VA, Kitao A, Matsunami H, Samatey FA Acta Crystallogr D Biol Crystallogr. 2013 May;69(Pt 5):812-20. doi:, 10.1107/S0907444913002102. Epub 2013 Apr 11. PMID:23633590<ref>PMID:23633590</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3b1s" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Flagellar biosynthetic protein|Flagellar biosynthetic protein]]
*[[Flagellar biosynthetic protein|Flagellar biosynthetic protein]]
*[[Flagellar protein 3D structures|Flagellar protein 3D structures]]
*[[Flagellar protein 3D structures|Flagellar protein 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Aquifex aeolicus huber and stetter 2001]]
[[Category: Aquifex aeolicus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Meshcheryakov, V A]]
[[Category: Meshcheryakov VA]]
[[Category: Samatey, F A]]
[[Category: Samatey FA]]
[[Category: Flagella]]
[[Category: Membrane protein]]
[[Category: Protein transport]]
[[Category: Type iii secretion system]]

Latest revision as of 14:03, 13 March 2024

Crystal structure of the cytoplasmic domain of FlhB from Aquifex aeolicus

3b1s, resolution 2.55Å

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