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New page: left|200px<br /><applet load="1orj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1orj, resolution 2.25Å" /> '''FLAGELLAR EXPORT CHA...
 
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[[Image:1orj.gif|left|200px]]<br /><applet load="1orj" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1orj, resolution 2.25&Aring;" />
'''FLAGELLAR EXPORT CHAPERONE'''<br />


==Overview==
==FLAGELLAR EXPORT CHAPERONE==
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.
<StructureSection load='1orj' size='340' side='right'caption='[[1orj]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
<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='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='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>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O67806_AQUAE O67806_AQUAE]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/or/1orj_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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>


==About this Structure==
==See Also==
1ORJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus_vf5 Aquifex aeolicus vf5]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ORJ OCA].
*[[Flagellar protein 3D structures|Flagellar protein 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12958592 12958592]
[[Category: Aquifex aeolicus VF5]]
[[Category: Aquifex aeolicus vf5]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Evdokimov AG]]
[[Category: Evdokimov, A.G.]]
[[Category: Peters III HK]]
[[Category: III, H.K.Peters.]]
[[Category: Phan J]]
[[Category: Phan, J.]]
[[Category: Pokross M]]
[[Category: Pokross, M.]]
[[Category: Routzahn KM]]
[[Category: Routzahn, K.M.]]
[[Category: Tropea JE]]
[[Category: Tropea, J.E.]]
[[Category: Waugh DS]]
[[Category: Waugh, D.S.]]
[[Category: chaperone]]
[[Category: flagellar export]]
[[Category: flagellin]]
[[Category: flagellum]]
[[Category: four helix bundle]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 01:19:24 2007''

Latest revision as of 11:02, 14 February 2024

FLAGELLAR EXPORT CHAPERONEFLAGELLAR EXPORT CHAPERONE

Structural highlights

1orj is a 4 chain structure with sequence from Aquifex aeolicus VF5. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.25Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

See Also

1orj, resolution 2.25Å

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