5yhf
From Proteopedia
(Difference between revisions)
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| - | ==Crystal structure of | + | ==Crystal structure of SecDF in Super-membrane-facing form== |
<StructureSection load='5yhf' size='340' side='right' caption='[[5yhf]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='5yhf' size='340' side='right' caption='[[5yhf]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5yhf]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YHF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YHF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5yhf]] is a 1 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=5YHF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YHF FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></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> | ||
<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=5yhf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yhf OCA], [http://pdbe.org/5yhf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yhf RCSB], [http://www.ebi.ac.uk/pdbsum/5yhf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yhf ProSAT]</span></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=5yhf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yhf OCA], [http://pdbe.org/5yhf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yhf RCSB], [http://www.ebi.ac.uk/pdbsum/5yhf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yhf ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == 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] | [[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] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The membrane protein SecDF, belonging to the RND superfamily, enhances protein translocation at the extracytoplasmic side using a proton gradient. Here, we report the crystal structure of SecDF in a form we named Super-membrane-facing (Super F) form, demonstrating a beta-barrel architecture instead of the previously reported beta-sheet structure. Through this structural insight and supporting results of an in vivo crosslinking experiment, we propose a remote coupling model in which a structural change of the transmembrane region drives a functional, extracytoplasmic conformational transition. | ||
| + | |||
| + | Remote Coupled Drastic beta-Barrel to beta-Sheet Transition of the Protein Translocation Motor.,Furukawa A, Nakayama S, Yoshikaie K, Tanaka Y, Tsukazaki T Structure. 2018 Jan 26. pii: S0969-2126(18)30002-9. doi:, 10.1016/j.str.2018.01.002. PMID:29398525<ref>PMID:29398525</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5yhf" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Thet8]] | ||
[[Category: Furukawa, A]] | [[Category: Furukawa, A]] | ||
[[Category: Tanaka, Y]] | [[Category: Tanaka, Y]] | ||
Revision as of 08:24, 22 February 2018
Crystal structure of SecDF in Super-membrane-facing form
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