1m6n: Difference between revisions

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New page: left|200px<br /><applet load="1m6n" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m6n, resolution 2.70Å" /> '''Crystal structure of...
 
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[[Image:1m6n.jpg|left|200px]]<br /><applet load="1m6n" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1m6n, resolution 2.70&Aring;" />
'''Crystal structure of the SecA translocation ATPase from Bacillus subtilis'''<br />


==Overview==
==Crystal structure of the SecA translocation ATPase from Bacillus subtilis==
The SecA adenosine triphosphatase (ATPase) mediates extrusion of the amino, termini of secreted proteins from the eubacterial cytosol based on cycles, of reversible binding to the SecYEG translocon. We have determined the, crystal structure of SecA with and without magnesium-adenosine diphosphate, bound to the high-affinity ATPase site at 3.0 and 2.7 angstrom resolution, respectively. Candidate sites for preprotein binding are located on a, surface containing the SecA epitopes exposed to the periplasm upon binding, to SecYEG and are thus positioned to deliver preprotein to SecYEG., Comparisons with structurally related ATPases, including superfamily I and, II ATP-dependent helicases, suggest that the interaction geometry of the, tandem motor domains in SecA is modulated by nucleotide binding, which is, shown by fluorescence anisotropy experiments to reverse an endothermic, domain-dissociation reaction hypothesized to gate binding to SecYEG.
<StructureSection load='1m6n' size='340' side='right'caption='[[1m6n]], [[Resolution|resolution]] 2.70&Aring;' 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]] 2.7&#8491;</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>


==About this Structure==
==See Also==
1M6N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M6N OCA].
*[[Preprotein translocase 3D structures|Preprotein translocase 3D structures]]
 
*[[SecA|SecA]]
==Reference==
__TOC__
Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA., Hunt JF, Weinkauf S, Henry L, Fak JJ, McNicholas P, Oliver DB, Deisenhofer J, Science. 2002 Sep 20;297(5589):2018-26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12242434 12242434]
</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Deisenhofer, J.]]
[[Category: Deisenhofer J]]
[[Category: Fak, J.J.]]
[[Category: Fak JJ]]
[[Category: Henry, L.]]
[[Category: Henry L]]
[[Category: Hunt, J.F.]]
[[Category: Hunt JF]]
[[Category: McNicholas, P.]]
[[Category: McNicholas P]]
[[Category: Oliver, D.B.]]
[[Category: Oliver DB]]
[[Category: Weinkauf, S.]]
[[Category: Weinkauf S]]
[[Category: SO4]]
[[Category: protein translocation; atpase; transmembrane transport; helicase family structure; mechanochemisty]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:11:12 2007''

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

1m6n is a 1 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.7Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1m6n, resolution 2.70Å

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