Proteopedia

1orj: Difference between revisions

← Older edit
No edit summary
No edit summary
 
Line 3: Line 3:
<StructureSection load='1orj' size='340' side='right'caption='[[1orj]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
<StructureSection load='1orj' size='340' side='right'caption='[[1orj]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1orj]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Aquae Aquae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ORJ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1ORJ FirstGlance]. <br>
<table><tr><td colspan='2'>[[1orj]] is a 4 chain structure with sequence from [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=1ORJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ORJ 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;'>[[1ory|1ory]]</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]] 2.25&#8491;</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])</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=1orj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1orj OCA], [https://pdbe.org/1orj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1orj RCSB], [https://www.ebi.ac.uk/pdbsum/1orj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1orj ProSAT]</span></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=1orj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1orj OCA], [http://pdbe.org/1orj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1orj RCSB], [http://www.ebi.ac.uk/pdbsum/1orj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1orj ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[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]]
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=1orj 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=1orj ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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<ref>PMID:12958592</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1orj" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Flagellar protein 3D structures|Flagellar protein 3D structures]]
*[[Flagellar protein 3D structures|Flagellar protein 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[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: Flagellar export]]
[[Category: Flagellin]]
[[Category: Flagellum]]
[[Category: Four helix bundle]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/w/1orj"