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2fsg

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{{Seed}}
 
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[[Image:2fsg.png|left|200px]]
 
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<!--
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==Complex SecA:ATP from Escherichia coli==
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The line below this paragraph, containing "STRUCTURE_2fsg", creates the "Structure Box" on the page.
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<StructureSection load='2fsg' size='340' side='right'caption='[[2fsg]], [[Resolution|resolution]] 2.20&Aring;' 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'>[[2fsg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FSG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FSG FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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{{STRUCTURE_2fsg| PDB=2fsg | SCENE= }}
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1tf5|1tf5]], [[1m6n|1m6n]], [[1nl3|1nl3]], [[2fsf|2fsf]], [[2fsh|2fsh]], [[2fsi|2fsi]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">secA, azi, pea, prlD ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=2fsg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fsg OCA], [https://pdbe.org/2fsg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fsg RCSB], [https://www.ebi.ac.uk/pdbsum/2fsg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fsg ProSAT]</span></td></tr>
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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>
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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/fs/2fsg_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=2fsg 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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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.
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===Complex SecA:ATP from Escherichia coli===
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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:17229438<ref>PMID:17229438</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 2fsg" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_17229438}}, adds the Publication Abstract to the page
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*[[Preprotein translocase|Preprotein translocase]]
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(as it appears on PubMed at http://www.pubmed.gov), where 17229438 is the PubMed ID number.
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*[[SecA|SecA]]
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-->
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== References ==
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{{ABSTRACT_PUBMED_17229438}}
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<references/>
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__TOC__
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==About this Structure==
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</StructureSection>
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2FSG is a [[Single protein]] structure of sequence 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=2FSG OCA].
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[[Category: Bacillus coli migula 1895]]
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[[Category: Large Structures]]
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==Reference==
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[[Category: Economou, A]]
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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://www.ncbi.nlm.nih.gov/pubmed/17229438 17229438]
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[[Category: Papanikolau, Y]]
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[[Category: Petratos, K]]
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Escherichia coli SecA truncated at its termini is functional and dimeric., Karamanou S, Sianidis G, Gouridis G, Pozidis C, Papanikolau Y, Papanikou E, Economou A, FEBS Lett. 2005 Feb 14;579(5):1267-71. Epub 2005 Jan 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15710424 15710424]
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[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Economou, A.]]
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[[Category: Papanikolau, Y.]]
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[[Category: Petratos, K.]]
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[[Category: Atpase]]
[[Category: Atpase]]
[[Category: Dna-rna helicase]]
[[Category: Dna-rna helicase]]
[[Category: Protein translocation]]
[[Category: Protein translocation]]
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[[Category: Protein transport]]
[[Category: Seca]]
[[Category: Seca]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:29:28 2008''
 

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Complex SecA:ATP from Escherichia coli

PDB ID 2fsg

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