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[[Image:2ipc.gif|left|200px]]


{{Structure
==Crystal structure of the translocation ATPase SecA from Thermus thermophilus reveals a parallel, head-to-head dimer==
|PDB= 2ipc |SIZE=350|CAPTION= <scene name='initialview01'>2ipc</scene>, resolution 2.8&Aring;
<StructureSection load='2ipc' size='340' side='right'caption='[[2ipc]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[2ipc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IPC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IPC FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
|GENE= SecA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 Thermus thermophilus])
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ipc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ipc OCA], [https://pdbe.org/2ipc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ipc RCSB], [https://www.ebi.ac.uk/pdbsum/2ipc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ipc ProSAT], [https://www.topsan.org/Proteins/RSGI/2ipc TOPSAN]</span></td></tr>
}}
</table>
== Function ==
[https://www.uniprot.org/uniprot/SECA_THET8 SECA_THET8] 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.[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/ip/2ipc_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=2ipc ConSurf].
<div style="clear:both"></div>


'''Crystal structure of the translocation ATPase SecA from Thermus thermophilus reveals a parallel, head-to-head dimer'''
==See Also==
 
*[[Preprotein translocase 3D structures|Preprotein translocase 3D structures]]
 
*[[SecA|SecA]]
==Overview==
__TOC__
The mechanism of pre-protein export through the bacterial cytoplasmic membrane, in which the SecA ATPase plays a crucial role as an "energy supplier", is poorly understood. In particular, biochemical and structural studies provide contradictory data as to the oligomeric state of SecA when it is integrated into the active trans-membrane translocase. Here, we report the 2.8 A resolution crystal structure of the Thermus thermophilus SecA protein (TtSecA). Whereas the structure of the TtSecA monomer closely resembles that from other bacteria, the oligomeric state of TtSecA is strikingly distinct. In contrast to the antiparallel (head-to-tail) dimerization reported previously for the other bacterial systems, TtSecA forms parallel (head-to-head) dimers that are reminiscent of open scissors. The dimer interface is abundant in bulky Arg and Lys side-chains from both subunits, which stack on one another to form an unusual "basic zipper" that is highly conserved, as revealed by homology modeling and sequence analysis. The basic zipper is sealed on both ends by two pairs of the salt bridges formed between the basic side-chains from the zipper and two invariant acidic residues. The organization of the dimers, in which the two pre-protein binding domains are located proximal to each other at the tip of the "scissors", might allow a concerted mode of substrate recognition while the opening/closing of the scissors might facilitate translocation.
</StructureSection>
 
[[Category: Large Structures]]
==About this Structure==
[[Category: Thermus thermophilus HB8]]
2IPC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IPC OCA].
[[Category: Ito K]]
 
[[Category: Kimura Y]]
==Reference==
[[Category: Mori H]]
Crystal structure of the translocation ATPase SecA from Thermus thermophilus reveals a parallel, head-to-head dimer., Vassylyev DG, Mori H, Vassylyeva MN, Tsukazaki T, Kimura Y, Tahirov TH, Ito K, J Mol Biol. 2006 Dec 1;364(3):248-58. Epub 2006 Sep 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17059823 17059823]
[[Category: Tahirov TH]]
[[Category: Single protein]]
[[Category: Tsukazaki T]]
[[Category: Thermus thermophilus]]
[[Category: Vassylyev DG]]
[[Category: Ito, K.]]
[[Category: Vassylyeva MN]]
[[Category: Kimura, Y.]]
[[Category: Mori, H.]]
[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
[[Category: Tahirov, T H.]]
[[Category: Tsukazaki, T.]]
[[Category: Vassylyev, D G.]]
[[Category: Vassylyeva, M N.]]
[[Category: atpase]]
[[Category: nucleotide binding fold]]
[[Category: parallel dimer]]
[[Category: riken structural genomics/proteomics initiative]]
[[Category: rsgi]]
[[Category: structural genomic]]
 
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Retrieved from "https://proteopedia.org/2ipc"