2vda

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[[Image:2vda.gif|left|200px]]
 
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==Solution structure of the SecA-signal peptide complex==
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The line below this paragraph, containing "STRUCTURE_2vda", creates the "Structure Box" on the page.
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<StructureSection load='2vda' size='340' side='right'caption='[[2vda]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2vda]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VDA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VDA FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1tm6|1tm6]], [[1tf5|1tf5]], [[1m6n|1m6n]], [[2fsf|2fsf]]</div></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vda FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vda OCA], [https://pdbe.org/2vda PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vda RCSB], [https://www.ebi.ac.uk/pdbsum/2vda PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vda ProSAT]</span></td></tr>
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{{STRUCTURE_2vda| PDB=2vda | SCENE= }}
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</table>
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== Function ==
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[[https://www.uniprot.org/uniprot/SECA_ECOLI SECA_ECOLI]] Required for protein export, interacts with the SecYEG preprotein conducting channel. SecA has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.<ref>PMID:15140892</ref> [[https://www.uniprot.org/uniprot/LAMB_ECOL6 LAMB_ECOL6]] Involved in the transport of maltose and maltodextrins (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vd/2vda_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2vda ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Recognition of signal sequences by cognate receptors controls the entry of virtually all proteins to export pathways. Despite its importance, this process remains poorly understood. Here, we present the solution structure of a signal peptide bound to SecA, the 204 kDa ATPase motor of the Sec translocase. Upon encounter, the signal peptide forms an alpha-helix that inserts into a flexible and elongated groove in SecA. The mode of binding is bimodal, with both hydrophobic and electrostatic interactions mediating recognition. The same groove is used by SecA to recognize a diverse set of signal sequences. Impairment of the signal-peptide binding to SecA results in significant translocation defects. The C-terminal tail of SecA occludes the groove and inhibits signal-peptide binding, but autoinhibition is relieved by the SecB chaperone. Finally, it is shown that SecA interconverts between two conformations in solution, suggesting a simple mechanism for polypeptide translocation.
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'''SOLUTION STRUCTURE OF THE SECA-SIGNAL PEPTIDE COMPLEX'''
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Structural basis for signal-sequence recognition by the translocase motor SecA as determined by NMR.,Gelis I, Bonvin AM, Keramisanou D, Koukaki M, Gouridis G, Karamanou S, Economou A, Kalodimos CG Cell. 2007 Nov 16;131(4):756-69. PMID:18022369<ref>PMID:18022369</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2vda" style="background-color:#fffaf0;"></div>
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==About this Structure==
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==See Also==
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2VDA is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VDA OCA].
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*[[Preprotein translocase|Preprotein translocase]]
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[[Category: Escherichia coli]]
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*[[SecA|SecA]]
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[[Category: Protein complex]]
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== References ==
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[[Category: Bonvin, A M.J J.]]
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<references/>
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[[Category: Economou, A.]]
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__TOC__
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[[Category: Gelis, I.]]
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</StructureSection>
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[[Category: Gouridis, G.]]
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[[Category: Bacillus coli migula 1895]]
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[[Category: Kalodimos, C G.]]
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[[Category: Large Structures]]
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[[Category: Karamanou, S.]]
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[[Category: Bonvin, A M.J J]]
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[[Category: Keramisanou, D.]]
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[[Category: Economou, A]]
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[[Category: Koukaki, M.]]
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[[Category: Gelis, I]]
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[[Category: Gouridis, G]]
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[[Category: Kalodimos, C G]]
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[[Category: Karamanou, S]]
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[[Category: Keramisanou, D]]
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[[Category: Koukaki, M]]
[[Category: Atp-binding]]
[[Category: Atp-binding]]
[[Category: High molecular weight complex]]
[[Category: High molecular weight complex]]
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[[Category: Transmembrane]]
[[Category: Transmembrane]]
[[Category: Transport]]
[[Category: Transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 18:37:39 2008''
 

Current revision

Solution structure of the SecA-signal peptide complex

PDB ID 2vda

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