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| | <StructureSection load='5xan' size='340' side='right'caption='[[5xan]], [[Resolution|resolution]] 2.75Å' scene=''> | | <StructureSection load='5xan' size='340' side='right'caption='[[5xan]], [[Resolution|resolution]] 2.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5xan]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Deira Deira]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XAN OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5XAN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5xan]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_radiodurans_R1 Deinococcus radiodurans R1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XAN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XAN FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=15P:POLYETHYLENE+GLYCOL+(N=34)'>15P</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5xam|5xam]], [[5xap|5xap]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=15P:POLYETHYLENE+GLYCOL+(N=34)'>15P</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">secD, secF, DR_1822 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243230 DEIRA])</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=5xan FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xan OCA], [https://pdbe.org/5xan PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xan RCSB], [https://www.ebi.ac.uk/pdbsum/5xan PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xan ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5xan FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xan OCA], [http://pdbe.org/5xan PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xan RCSB], [http://www.ebi.ac.uk/pdbsum/5xan PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xan ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Q9RTE3_DEIRA Q9RTE3_DEIRA]] 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_01464][SAAS:SAAS00541769] | + | [https://www.uniprot.org/uniprot/Q9RTE3_DEIRA Q9RTE3_DEIRA] 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_01464][SAAS:SAAS00541769] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Deira]] | + | [[Category: Deinococcus radiodurans R1]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Furukwa, A]] | + | [[Category: Furukwa A]] |
| - | [[Category: Tanaka, Y]] | + | [[Category: Tanaka Y]] |
| - | [[Category: Tsukazaki, T]] | + | [[Category: Tsukazaki T]] |
| - | [[Category: Alfa helical]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Sec translocon]]
| + | |
| Structural highlights
Function
Q9RTE3_DEIRA 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_01464][SAAS:SAAS00541769]
Publication Abstract from PubMed
Protein secretion mediated by SecYEG translocon and SecA ATPase is enhanced by membrane-embedded SecDF by using proton motive force. A previous structural study of SecDF indicated that it comprises 12 transmembrane helices that can conduct protons and three periplasmic domains, which form at least two characterized transition states, termed the F and I forms. We report the structures of full-length SecDF in I form at 2.6- to 2.8-A resolution. The structures revealed that SecDF in I form can generate a tunnel that penetrates the transmembrane region and functions as a proton pathway regulated by a conserved Asp residue of the transmembrane region. In one crystal structure, periplasmic cavity interacts with a molecule, potentially polyethylene glycol, which may mimic a substrate peptide. This study provides structural insights into the Sec protein translocation that allows future analyses to develop a more detailed working model for SecDF.
Tunnel Formation Inferred from the I-Form Structures of the Proton-Driven Protein Secretion Motor SecDF.,Furukawa A, Yoshikaie K, Mori T, Mori H, Morimoto YV, Sugano Y, Iwaki S, Minamino T, Sugita Y, Tanaka Y, Tsukazaki T Cell Rep. 2017 May 2;19(5):895-901. doi: 10.1016/j.celrep.2017.04.030. PMID:28467902[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Furukawa A, Yoshikaie K, Mori T, Mori H, Morimoto YV, Sugano Y, Iwaki S, Minamino T, Sugita Y, Tanaka Y, Tsukazaki T. Tunnel Formation Inferred from the I-Form Structures of the Proton-Driven Protein Secretion Motor SecDF. Cell Rep. 2017 May 2;19(5):895-901. doi: 10.1016/j.celrep.2017.04.030. PMID:28467902 doi:http://dx.doi.org/10.1016/j.celrep.2017.04.030
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