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New page: left|200px<br /><applet load="2fsf" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fsf, resolution 2.000Å" /> '''Escherichia coli Se...
 
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[[Image:2fsf.jpg|left|200px]]<br /><applet load="2fsf" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2fsf, resolution 2.000&Aring;" />
'''Escherichia coli SecA, the preprotein translocase dimeric ATPase'''<br />


==Overview==
==Escherichia coli SecA, the preprotein translocase dimeric ATPase==
SecA is the preprotein translocase ATPase subunit and a superfamily 2, (SF2) RNA helicase. Here we present the 2 A crystal structures of the, Escherichia coli SecA homodimer in the apo form and in complex with ATP, ADP and adenosine 5'-[beta,gamma-imido]triphosphate (AMP-PNP). Each, monomer contains the SF2 ATPase core (DEAD motor) built of two domains, (nucleotide binding domain, NBD and intramolecular regulator of ATPase 2, IRA2), the preprotein binding domain (PBD), which is inserted in NBD and a, carboxy-terminal domain (C-domain) linked to IRA2. The structures of the, nucleotide complexes of SecA identify an interfacial nucleotide-binding, cleft located between the two DEAD motor domains and residues critical for, ATP catalysis. The dimer comprises two virtually identical protomers, associating in an antiparallel fashion. Dimerization is mediated solely, through extensive contacts of the DEAD motor domains leaving the C-domain, facing outwards from the dimerization core. This dimerization mode, explains the effect of functionally important mutations and is completely, different from the dimerization models proposed for other SecA structures., The repercussion of these findings on translocase assembly and catalysis, is discussed.
<StructureSection load='2fsf' size='340' side='right'caption='[[2fsf]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2fsf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FSF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FSF 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&#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=2fsf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fsf OCA], [https://pdbe.org/2fsf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fsf RCSB], [https://www.ebi.ac.uk/pdbsum/2fsf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fsf ProSAT]</span></td></tr>
</table>
== Function ==
[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>
== 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/fs/2fsf_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=2fsf ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2FSF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FSF OCA].
*[[Preprotein translocase 3D structures|Preprotein translocase 3D structures]]
 
*[[SecA|SecA]]
==Reference==
== References ==
Structure of dimeric SecA, the Escherichia coli preprotein translocase motor., Papanikolau Y, Papadovasilaki M, Ravelli RB, McCarthy AA, Cusack S, Economou A, Petratos K, J Mol Biol. 2007 Mar 9;366(5):1545-57. Epub 2006 Dec 23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17229438 17229438]
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Economou, A.]]
[[Category: Economou A]]
[[Category: Papanikolau, Y.]]
[[Category: Papanikolau Y]]
[[Category: Petratos, K.]]
[[Category: Petratos K]]
[[Category: atpase]]
[[Category: dna-rna helicase]]
[[Category: protein translocation]]
[[Category: seca]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:44:12 2007''

Latest revision as of 13:51, 13 March 2024

Escherichia coli SecA, the preprotein translocase dimeric ATPase

2fsf, resolution 2.00Å

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