2vda

From Proteopedia

(Difference between revisions)

Revision as of 19:03, 24 January 2018

Warning: this is a large structure, and loading might take a long time or not happen at all.

Solution structure of the SecA-signal peptide complex

Structural highlights

2vda is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1tm6, 1tf5, 1m6n, 2fsf
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Warning: this is a large structure, and loading might take a long time or not happen at all.

Function

[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.^[1] [LAMB_ECOL6] Involved in the transport of maltose and maltodextrins (By similarity).

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

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.

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Froderberg L, Houben EN, Baars L, Luirink J, de Gier JW. Targeting and translocation of two lipoproteins in Escherichia coli via the SRP/Sec/YidC pathway. J Biol Chem. 2004 Jul 23;279(30):31026-32. Epub 2004 May 12. PMID:15140892 doi:10.1074/jbc.M403229200
↑ Gelis I, Bonvin AM, Keramisanou D, Koukaki M, Gouridis G, Karamanou S, Economou A, Kalodimos CG. Structural basis for signal-sequence recognition by the translocase motor SecA as determined by NMR. Cell. 2007 Nov 16;131(4):756-69. PMID:18022369 doi:S0092-8674(07)01269-X

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2vda"

@@ Line 1: / Line 1: @@
-==SOLUTION STRUCTURE OF THE SECA-SIGNAL PEPTIDE COMPLEX==
+{{Large structure}}
+==Solution structure of the SecA-signal peptide complex==
 <StructureSection load='2vda' size='340' side='right' caption='[[2vda]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2vda]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VDA FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1tm6|1tm6]], [[1tf5|1tf5]], [[1m6n|1m6n]], [[2fsf|2fsf]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vda FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vda OCA], [http://pdbe.org/2vda PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vda RCSB], [http://www.ebi.ac.uk/pdbsum/2vda PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vda FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vda OCA], [http://pdbe.org/2vda PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vda RCSB], [http://www.ebi.ac.uk/pdbsum/2vda PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vda ProSAT]</span></td></tr>
 </table>
 {{Large structure}}
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vd/2vda_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vd/2vda_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 28: / Line 29: @@
 </div>
 <div class="pdbe-citations 2vda" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Preprotein translocase|Preprotein translocase]]
-*[[SecA|SecA]]
 == References ==
 <references/>

2vda

From Proteopedia

Revision as of 19:03, 24 January 2018

Solution structure of the SecA-signal peptide complex

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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