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| | <SX load='5mg3' size='340' side='right' viewer='molstar' caption='[[5mg3]], [[Resolution|resolution]] 14.00Å' scene=''> | | <SX load='5mg3' size='340' side='right' viewer='molstar' caption='[[5mg3]], [[Resolution|resolution]] 14.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5mg3]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MG3 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5MG3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5mg3]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MG3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MG3 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">secY, prlA, b3300, JW3262 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895]), secE, prlG, b3981, JW3944 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895]), secG, b3175, JW3142 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895]), secD, b0408, JW0398 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895]), secF, b0409, JW0399 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895]), yidC, b3705, JW3683 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 14Å</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=5mg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mg3 OCA], [http://pdbe.org/5mg3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mg3 RCSB], [http://www.ebi.ac.uk/pdbsum/5mg3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mg3 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=5mg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mg3 OCA], [https://pdbe.org/5mg3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mg3 RCSB], [https://www.ebi.ac.uk/pdbsum/5mg3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mg3 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/YIDC_ECOLI YIDC_ECOLI]] Inner membrane protein required for the insertion and/or proper folding and/or complex formation of integral inner membrane proteins. Involved in integration of membrane proteins that insert dependently and independently of the Sec translocase complex, as well as at least 2 lipoproteins. Its own insertion requires SRP and is Sec translocase-dependent. Essential for the integration of Sec-dependent subunit a of the F(0)ATP synthase, FtsQ and SecE proteins and for Sec-independent subunit c of the F(0)ATP synthase, M13 phage procoat and the N-terminus of leader peptidase Lep. Probably interacts directly with Sec-independent substrates. Sec-dependent protein FtsQ interacts first with SecY then subsequently with YidC. Sec-dependent LacY and MalF require YidC to acquire tertiary structure and stability, a chaperone-like function, but not for membrane insertion. Stable maltose transport copmplex formation (MalFGK(2)) also requires YidC. Partially complements a Streptococcus mutans yidC2 disruption mutant.<ref>PMID:10675323</ref> <ref>PMID:10949305</ref> <ref>PMID:12724529</ref> <ref>PMID:12950181</ref> <ref>PMID:15140892</ref> <ref>PMID:15067017</ref> <ref>PMID:17073462</ref> <ref>PMID:18456666</ref> [[http://www.uniprot.org/uniprot/SECD_ECOLI SECD_ECOLI]] 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. The large periplasmic domain is thought to have a base and head domain joined by a hinge; movement of the hinge may be coupled to both proton transport and protein export, with the head domain capturing substrate, and a conformational change preventing backward movement and driving forward movement. Expression of V.alginolyticus SecD and SecF in E.coli confers Na(+)-dependent protein export, strongly suggesting SecDF functions via cation-coupled protein translocation.<ref>PMID:21562494</ref> [[http://www.uniprot.org/uniprot/SECY_ECOLI SECY_ECOLI]] 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. SecY is required to insert newly synthesized SecY into the inner membrane. Overexpression of some hybrid proteins has been thought to jam the protein secretion apparatus resulting in cell death; while this may be true, overexpression also results in FtsH-mediated degradation of SecY.[HAMAP-Rule:MF_01465] [[http://www.uniprot.org/uniprot/SECG_ECOLI SECG_ECOLI]] Subunit of the protein translocation channel SecYEG. Overexpression of some hybrid proteins has been thought to jam the protein secretion apparatus resulting in cell death; while this may be true it also results in FtsH-mediated degradation of SecY. Treatment with antibiotics that block translation elongation such as chloramphenicol also leads to degradation of SecY and SecE but not SecG. [[http://www.uniprot.org/uniprot/SECE_ECOLI SECE_ECOLI]] Essential subunit of the protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation. Overexpression of some hybrid proteins has been thought to jam the protein secretion apparatus resulting in cell death; while this may be true it also results in FtsH-mediated degradation of SecY.<ref>PMID:15140892</ref> [[http://www.uniprot.org/uniprot/SECF_ECOLI SECF_ECOLI]] 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. The large periplasmic domain is thought to have a base and head domain joined by a hinge; movement of the hinge may be coupled to both proton transport and protein export, with the head domain capturing substrate, and a conformational change preventing backward movement and driving forward movement. Expression of V.alginolyticus SecD and SecF in E.coli confers Na(+)-dependent protein export, strongly suggesting SecDF functions via cation-coupled protein translocation.<ref>PMID:21562494</ref> | + | [https://www.uniprot.org/uniprot/SECY_ECOLI SECY_ECOLI] 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. SecY is required to insert newly synthesized SecY into the inner membrane. Overexpression of some hybrid proteins has been thought to jam the protein secretion apparatus resulting in cell death; while this may be true, overexpression also results in FtsH-mediated degradation of SecY.[HAMAP-Rule:MF_01465] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| | *[[Insertase|Insertase]] | | *[[Insertase|Insertase]] |
| - | *[[Preprotein translocase|Preprotein translocase]] | + | *[[Preprotein translocase 3D structures|Preprotein translocase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </SX> | | </SX> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Botte, M]] | + | [[Category: Botte M]] |
| - | [[Category: Schaffitzel, C]] | + | [[Category: Schaffitzel C]] |
| - | [[Category: Chaperone]]
| + | |
| - | [[Category: Holotranslocon]]
| + | |
| - | [[Category: Membrane protein insertion machinery]]
| + | |
| - | [[Category: Protein secretion]]
| + | |
| Structural highlights
Function
SECY_ECOLI 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. SecY is required to insert newly synthesized SecY into the inner membrane. Overexpression of some hybrid proteins has been thought to jam the protein secretion apparatus resulting in cell death; while this may be true, overexpression also results in FtsH-mediated degradation of SecY.[HAMAP-Rule:MF_01465]
Publication Abstract from PubMed
The conserved SecYEG protein-conducting channel and the accessory proteins SecDF-YajC and YidC constitute the bacterial holo-translocon (HTL), capable of protein-secretion and membrane-protein insertion. By employing an integrative approach combining small-angle neutron scattering (SANS), low-resolution electron microscopy and biophysical analyses we determined the arrangement of the proteins and lipids within the super-complex. The results guided the placement of X-ray structures of individual HTL components and allowed the proposal of a model of the functional translocon. Their arrangement around a central lipid-containing pool conveys an unexpected, but compelling mechanism for membrane-protein insertion. The periplasmic domains of YidC and SecD are poised at the protein-channel exit-site of SecY, presumably to aid the emergence of translocating polypeptides. The SecY lateral gate for membrane-insertion is adjacent to the membrane 'insertase' YidC. Absolute-scale SANS employing a novel contrast-match-point analysis revealed a dynamic complex adopting open and compact configurations around an adaptable central lipid-filled chamber, wherein polytopic membrane-proteins could fold, sheltered from aggregation and proteolysis.
A central cavity within the holo-translocon suggests a mechanism for membrane protein insertion.,Botte M, Zaccai NR, Nijeholt JL, Martin R, Knoops K, Papai G, Zou J, Deniaud A, Karuppasamy M, Jiang Q, Roy AS, Schulten K, Schultz P, Rappsilber J, Zaccai G, Berger I, Collinson I, Schaffitzel C Sci Rep. 2016 Dec 7;6:38399. doi: 10.1038/srep38399. PMID:27924919[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Botte M, Zaccai NR, Nijeholt JL, Martin R, Knoops K, Papai G, Zou J, Deniaud A, Karuppasamy M, Jiang Q, Roy AS, Schulten K, Schultz P, Rappsilber J, Zaccai G, Berger I, Collinson I, Schaffitzel C. A central cavity within the holo-translocon suggests a mechanism for membrane protein insertion. Sci Rep. 2016 Dec 7;6:38399. doi: 10.1038/srep38399. PMID:27924919 doi:http://dx.doi.org/10.1038/srep38399
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