1m6n: Difference between revisions
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== | ==Crystal structure of the SecA translocation ATPase from Bacillus subtilis== | ||
[[1m6n]] is a 1 chain structure with sequence from [ | <StructureSection load='1m6n' size='340' side='right'caption='[[1m6n]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1m6n]] 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=1M6N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M6N 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]] 2.7Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1m6n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m6n OCA], [https://pdbe.org/1m6n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m6n RCSB], [https://www.ebi.ac.uk/pdbsum/1m6n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m6n ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[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] | |||
== 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/m6/1m6n_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=1m6n ConSurf]. | |||
<div style="clear:both"></div> | |||
==See Also== | ==See Also== | ||
*[[Preprotein translocase 3D structures|Preprotein translocase 3D structures]] | |||
*[[SecA|SecA]] | *[[SecA|SecA]] | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Deisenhofer | [[Category: Large Structures]] | ||
[[Category: Fak | [[Category: Deisenhofer J]] | ||
[[Category: Henry | [[Category: Fak JJ]] | ||
[[Category: Hunt | [[Category: Henry L]] | ||
[[Category: McNicholas | [[Category: Hunt JF]] | ||
[[Category: Oliver | [[Category: McNicholas P]] | ||
[[Category: Weinkauf | [[Category: Oliver DB]] | ||
[[Category: Weinkauf S]] | |||
Latest revision as of 10:40, 14 February 2024
Crystal structure of the SecA translocation ATPase from Bacillus subtilisCrystal structure of the SecA translocation ATPase from Bacillus subtilis
Structural highlights
FunctionSECA_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] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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