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3aqo

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Revision as of 15:01, 29 December 2021

Structure and function of a membrane component SecDF that enhances protein export

Structural highlights

3aqo is a 4 chain structure with sequence from Thet8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	secDF, TTHA0697 (THET8)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SECDF_THET8] Conducts protons, which can be regulated by a proton gradient or by binding of an unfolded protein. Proton conduction requires the large periplasmic domain of the SecD.[HAMAP-Rule:MF_01463_B] Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.[HAMAP-Rule:MF_01463_B]

Publication Abstract from PubMed

Protein translocation across the bacterial membrane, mediated by the secretory translocon SecYEG and the SecA ATPase, is enhanced by proton motive force and membrane-integrated SecDF, which associates with SecYEG. The role of SecDF has remained unclear, although it is proposed to function in later stages of translocation as well as in membrane protein biogenesis. Here, we determined the crystal structure of Thermus thermophilus SecDF at 3.3 A resolution, revealing a pseudo-symmetrical, 12-helix transmembrane domain belonging to the RND superfamily and two major periplasmic domains, P1 and P4. Higher-resolution analysis of the periplasmic domains suggested that P1, which binds an unfolded protein, undergoes functionally important conformational changes. In vitro analyses identified an ATP-independent step of protein translocation that requires both SecDF and proton motive force. Electrophysiological analyses revealed that SecDF conducts protons in a manner dependent on pH and the presence of an unfolded protein, with conserved Asp and Arg residues at the transmembrane interface between SecD and SecF playing essential roles in the movements of protons and preproteins. Therefore, we propose that SecDF functions as a membrane-integrated chaperone, powered by proton motive force, to achieve ATP-independent protein translocation.

Structure and function of a membrane component SecDF that enhances protein export.,Tsukazaki T, Mori H, Echizen Y, Ishitani R, Fukai S, Tanaka T, Perederina A, Vassylyev DG, Kohno T, Maturana AD, Ito K, Nureki O Nature. 2011 May 11;474(7350):235-8. doi: 10.1038/nature09980. PMID:21562494^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Tsukazaki T, Mori H, Echizen Y, Ishitani R, Fukai S, Tanaka T, Perederina A, Vassylyev DG, Kohno T, Maturana AD, Ito K, Nureki O. Structure and function of a membrane component SecDF that enhances protein export. Nature. 2011 May 11;474(7350):235-8. doi: 10.1038/nature09980. PMID:21562494 doi:10.1038/nature09980

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3aqo"

@@ Line 1: / Line 1: @@
 ==Structure and function of a membrane component SecDF that enhances protein export==
-<StructureSection load='3aqo' size='340' side='right' caption='[[3aqo]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+<StructureSection load='3aqo' size='340' side='right'caption='[[3aqo]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3aqo]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet8 Thet8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AQO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AQO FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3aqo]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thet8 Thet8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AQO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AQO FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">secDF, TTHA0697 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300852 THET8])</td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">secDF, TTHA0697 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300852 THET8])</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=3aqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aqo OCA], [http://pdbe.org/3aqo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3aqo RCSB], [http://www.ebi.ac.uk/pdbsum/3aqo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3aqo ProSAT]</span></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=3aqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aqo OCA], [https://pdbe.org/3aqo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aqo RCSB], [https://www.ebi.ac.uk/pdbsum/3aqo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aqo ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SECDF_THET8 SECDF_THET8]] Conducts protons, which can be regulated by a proton gradient or by binding of an unfolded protein. Proton conduction requires the large periplasmic domain of the SecD.[HAMAP-Rule:MF_01463_B]  Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.[HAMAP-Rule:MF_01463_B]
+[[https://www.uniprot.org/uniprot/SECDF_THET8 SECDF_THET8]] Conducts protons, which can be regulated by a proton gradient or by binding of an unfolded protein. Proton conduction requires the large periplasmic domain of the SecD.[HAMAP-Rule:MF_01463_B]  Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.[HAMAP-Rule:MF_01463_B]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 22: @@
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Thet8]]
 [[Category: Echizen, Y]]

3aqo

From Proteopedia

Revision as of 15:01, 29 December 2021

Structure and function of a membrane component SecDF that enhances protein export

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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