3dl8

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
{{STRUCTURE_3dl8| PDB=3dl8 | SCENE= }}
+
==Structure of the complex of aquifex aeolicus SecYEG and bacillus subtilis SecA==
-
===Structure of the complex of aquifex aeolicus SecYEG and bacillus subtilis SecA===
+
<StructureSection load='3dl8' size='340' side='right' caption='[[3dl8]], [[Resolution|resolution]] 7.50&Aring;' scene=''>
-
{{ABSTRACT_PUBMED_18923516}}
+
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[3dl8]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus] and [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DL8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3DL8 FirstGlance]. <br>
 +
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">secA, div+, BSU35300 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]), secY, aq_079 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=63363 Aquifex aeolicus]), secG, aq_098 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=63363 Aquifex aeolicus])</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=3dl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dl8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3dl8 RCSB], [http://www.ebi.ac.uk/pdbsum/3dl8 PDBsum]</span></td></tr>
 +
</table>
 +
== 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/dl/3dl8_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/chain_selection.php?pdb_ID=2ata ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Most proteins are secreted from bacteria by the interaction of the cytoplasmic SecA ATPase with a membrane channel, formed by the heterotrimeric SecY complex. Here we report the crystal structure of SecA bound to the SecY complex, with a maximum resolution of 4.5 angstrom (A), obtained for components from Thermotoga maritima. One copy of SecA in an intermediate state of ATP hydrolysis is bound to one molecule of the SecY complex. Both partners undergo important conformational changes on interaction. The polypeptide-cross-linking domain of SecA makes a large conformational change that could capture the translocation substrate in a 'clamp'. Polypeptide movement through the SecY channel could be achieved by the motion of a 'two-helix finger' of SecA inside the cytoplasmic funnel of SecY, and by the coordinated tightening and widening of SecA's clamp above the SecY pore. SecA binding generates a 'window' at the lateral gate of the SecY channel and it displaces the plug domain, preparing the channel for signal sequence binding and channel opening.
-
==Function==
+
Structure of a complex of the ATPase SecA and the protein-translocation channel.,Zimmer J, Nam Y, Rapoport TA Nature. 2008 Oct 16;455(7215):936-43. PMID:18923516<ref>PMID:18923516</ref>
-
[[http://www.uniprot.org/uniprot/SECG_AQUAE SECG_AQUAE]] Subunit of the protein translocation channel SecYEG. [[http://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] [[http://www.uniprot.org/uniprot/SECY_AQUAE SECY_AQUAE]] The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently (By similarity).
+
-
==About this Structure==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
[[3dl8]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus] and [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DL8 OCA].
+
</div>
==See Also==
==See Also==
*[[Preprotein translocase|Preprotein translocase]]
*[[Preprotein translocase|Preprotein translocase]]
*[[SecA|SecA]]
*[[SecA|SecA]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
<ref group="xtra">PMID:018923516</ref><references group="xtra"/><references/>
+
__TOC__
 +
</StructureSection>
[[Category: Aquifex aeolicus]]
[[Category: Aquifex aeolicus]]
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
-
[[Category: Nam, Y.]]
+
[[Category: Nam, Y]]
-
[[Category: Rapoport, T A.]]
+
[[Category: Rapoport, T A]]
-
[[Category: Zimmer, J.]]
+
[[Category: Zimmer, J]]
[[Category: Atp-binding]]
[[Category: Atp-binding]]
[[Category: Cell membrane]]
[[Category: Cell membrane]]

Revision as of 14:05, 18 December 2014

Structure of the complex of aquifex aeolicus SecYEG and bacillus subtilis SecA

3dl8, resolution 7.50Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3dl8"
Personal tools