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''' | ==Crystal structure of the accessory translocation ATPase, SecA2, from Mycobacterium tuberculosis== | ||
<StructureSection load='4uaq' size='340' side='right' caption='[[4uaq]], [[Resolution|resolution]] 2.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4uaq]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UAQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UAQ FirstGlance]. <br> | |||
</td></tr><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> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4uaq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uaq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4uaq RCSB], [http://www.ebi.ac.uk/pdbsum/4uaq PDBsum]</span></td></tr> | |||
</table> | |||
[[ | == Function == | ||
[[http://www.uniprot.org/uniprot/SECA2_MYCTU SECA2_MYCTU]] 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. | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Braunstein, M]] | [[Category: Braunstein, M]] | ||
[[Category: Miller, B | [[Category: Ioerger, T R]] | ||
[[Category: | [[Category: Miller, B K]] | ||
[[Category: | [[Category: Rigel, N W]] | ||
[[Category: Sacchettini, J C]] | |||
[[Category: Swanson-Smith, S]] | [[Category: Swanson-Smith, S]] | ||
[[Category: | [[Category: Structural genomic]] | ||
[[Category: | [[Category: Dead/deah box helicase preprotein translocation atp binding seca preprotein cross-linking domain]] | ||
[[Category: PSI, Protein structure initiative]] | |||
[[Category: Protein transport]] | |||
[[Category: Tbsgc]] | |||
Revision as of 14:18, 9 September 2015
Crystal structure of the accessory translocation ATPase, SecA2, from Mycobacterium tuberculosisCrystal structure of the accessory translocation ATPase, SecA2, from Mycobacterium tuberculosis
Structural highlights
Function[SECA2_MYCTU] 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. |
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