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| | <StructureSection load='1ory' size='340' side='right'caption='[[1ory]], [[Resolution|resolution]] 2.45Å' scene=''> | | <StructureSection load='1ory' size='340' side='right'caption='[[1ory]], [[Resolution|resolution]] 2.45Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1ory]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"aquifex_aeolicus"_huber_and_stetter_2001 "aquifex aeolicus" huber and stetter 2001] and [http://en.wikipedia.org/wiki/Aquae Aquae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ORY OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1ORY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1ory]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus] and [https://en.wikipedia.org/wiki/Aquifex_aeolicus_VF5 Aquifex aeolicus VF5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ORY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ORY FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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]] 2.45Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FliS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224324 AQUAE]), FLAA OR FLIC OR AQ_1998 ([http://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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1ory FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ory OCA], [http://pdbe.org/1ory PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ory RCSB], [http://www.ebi.ac.uk/pdbsum/1ory PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ory 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=1ory FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ory OCA], [https://pdbe.org/1ory PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ory RCSB], [https://www.ebi.ac.uk/pdbsum/1ory PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ory ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FLAA_AQUAE FLAA_AQUAE]] Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | + | [https://www.uniprot.org/uniprot/O67806_AQUAE O67806_AQUAE] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aquifex aeolicus huber and stetter 2001]] | + | [[Category: Aquifex aeolicus]] |
| - | [[Category: Aquae]] | + | [[Category: Aquifex aeolicus VF5]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Evdokimov, A G]] | + | [[Category: Evdokimov AG]] |
| - | [[Category: III, H K.Peters]] | + | [[Category: Peters III HK]] |
| - | [[Category: Phan, J]] | + | [[Category: Phan J]] |
| - | [[Category: Pokross, M]] | + | [[Category: Pokross M]] |
| - | [[Category: Routzahn, K M]] | + | [[Category: Routzahn KM]] |
| - | [[Category: Tropea, J E]] | + | [[Category: Tropea JE]] |
| - | [[Category: Waugh, D S]] | + | [[Category: Waugh DS]] |
| - | [[Category: Chaperone]]
| + | |
| - | [[Category: Cytosolic export chaperone]]
| + | |
| - | [[Category: Flagellar chaperone]]
| + | |
| - | [[Category: Flagellin]]
| + | |
| - | [[Category: Fli]]
| + | |
| - | [[Category: Flic]]
| + | |
| Structural highlights
Function
O67806_AQUAE
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Assembly of the bacterial flagellum and type III secretion in pathogenic bacteria require cytosolic export chaperones that interact with mobile components to facilitate their secretion. Although their amino acid sequences are not conserved, the structures of several type III secretion chaperones revealed striking similarities between their folds and modes of substrate recognition. Here, we report the first crystallographic structure of a flagellar export chaperone, Aquifex aeolicus FliS. FliS adopts a novel fold that is clearly distinct from those of the type III secretion chaperones, indicating that they do not share a common evolutionary origin. However, the structure of FliS in complex with a fragment of FliC (flagellin) reveals that, like the type III secretion chaperones, flagellar export chaperones bind their target proteins in extended conformation and suggests that this mode of recognition may be widely used in bacteria.
Similar modes of polypeptide recognition by export chaperones in flagellar biosynthesis and type III secretion.,Evdokimov AG, Phan J, Tropea JE, Routzahn KM, Peters HK, Pokross M, Waugh DS Nat Struct Biol. 2003 Oct;10(10):789-93. Epub 2003 Sep 7. PMID:12958592[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Evdokimov AG, Phan J, Tropea JE, Routzahn KM, Peters HK, Pokross M, Waugh DS. Similar modes of polypeptide recognition by export chaperones in flagellar biosynthesis and type III secretion. Nat Struct Biol. 2003 Oct;10(10):789-93. Epub 2003 Sep 7. PMID:12958592 doi:http://dx.doi.org/10.1038/nsb982
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