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1tf5

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[[Image:1tf5.jpg|left|200px]]
 
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==Crystal structure of SecA in an open conformation from Bacillus Subtilis==
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The line below this paragraph, containing "STRUCTURE_1tf5", creates the "Structure Box" on the page.
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<StructureSection load='1tf5' size='340' side='right'caption='[[1tf5]], [[Resolution|resolution]] 2.18&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'>[[1tf5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TF5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TF5 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.18&#8491;</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=1tf5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tf5 OCA], [https://pdbe.org/1tf5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tf5 RCSB], [https://www.ebi.ac.uk/pdbsum/1tf5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tf5 ProSAT]</span></td></tr>
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{{STRUCTURE_1tf5| PDB=1tf5 | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SECA_BACSU SECA_BACSU] Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane (By similarity).[HAMAP-Rule:MF_01382]
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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/tf/1tf5_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=1tf5 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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The ATPase SecA mediates the posttranslational translocation of a wide range of polypeptide substrates through the SecY channel in the cytoplasmic membrane of bacteria. We have determined the crystal structure of a monomeric form of Bacillus subtilis SecA at a 2.2-A resolution. A comparison with the previously determined structures of SecA reveals a nucleotide-independent, large conformational change that opens a deep groove similar to that in other proteins that interact with diverse polypeptides. We propose that the open form of SecA represents an activated state.
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'''Crystal structure of SecA in an open conformation from Bacillus Subtilis'''
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A large conformational change of the translocation ATPase SecA.,Osborne AR, Clemons WM Jr, Rapoport TA Proc Natl Acad Sci U S A. 2004 Jul 27;101(30):10937-42. Epub 2004 Jul 15. PMID:15256599<ref>PMID:15256599</ref>
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==Overview==
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The ATPase SecA mediates the posttranslational translocation of a wide range of polypeptide substrates through the SecY channel in the cytoplasmic membrane of bacteria. We have determined the crystal structure of a monomeric form of Bacillus subtilis SecA at a 2.2-A resolution. A comparison with the previously determined structures of SecA reveals a nucleotide-independent, large conformational change that opens a deep groove similar to that in other proteins that interact with diverse polypeptides. We propose that the open form of SecA represents an activated state.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1TF5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TF5 OCA].
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</div>
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<div class="pdbe-citations 1tf5" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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A large conformational change of the translocation ATPase SecA., Osborne AR, Clemons WM Jr, Rapoport TA, Proc Natl Acad Sci U S A. 2004 Jul 27;101(30):10937-42. Epub 2004 Jul 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15256599 15256599]
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*[[Preprotein translocase|Preprotein translocase]]
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*[[SecA|SecA]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Jr., W M.Clemons.]]
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[[Category: Clemons Jr WM]]
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[[Category: Osborne, A R.]]
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[[Category: Osborne AR]]
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[[Category: Rapoport, T A.]]
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[[Category: Rapoport TA]]
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[[Category: Atpase]]
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[[Category: Helicase]]
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[[Category: Secretion]]
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[[Category: Translocation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:52:42 2008''
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Current revision

Crystal structure of SecA in an open conformation from Bacillus Subtilis

PDB ID 1tf5

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