5m5h: Difference between revisions

Latest revision as of 21:26, 1 November 2023

RIBOSOME-BOUND YIDC INSERTASERIBOSOME-BOUND YIDC INSERTASE

5m5h, resolution 4.50Å

Structural highlights

5m5h is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 4.5Å
Experimental data:	Check
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8]

Publication Abstract from PubMed

Members of the YidC/Oxa1/Alb3 family universally facilitate membrane protein biogenesis, via mechanisms that have thus far remained unclear. Here, we investigated two crucial functional aspects: the interaction of YidC with ribosome:nascent chain complexes (RNCs) and the structural dynamics of RNC-bound YidC in nanodiscs. We observed that a fully exposed nascent transmembrane domain (TMD) is required for high-affinity YidC:RNC interactions, while weaker binding may already occur at earlier stages of translation. YidC efficiently catalyzed the membrane insertion of nascent TMDs in both fluid and gel phase membranes. Cryo-electron microscopy and fluorescence analysis revealed a conformational change in YidC upon nascent chain insertion: the essential TMDs 2 and 3 of YidC were tilted, while the amphipathic helix EH1 relocated into the hydrophobic core of the membrane. We suggest that EH1 serves as a mechanical lever, facilitating a coordinated movement of YidC TMDs to trigger the release of nascent chains into the membrane.

Structural Dynamics of the YidC:Ribosome Complex during Membrane Protein Biogenesis.,Kedrov A, Wickles S, Crevenna AH, van der Sluis EO, Buschauer R, Berninghausen O, Lamb DC, Beckmann R Cell Rep. 2016 Dec 13;17(11):2943-2954. doi: 10.1016/j.celrep.2016.11.059. PMID:27974208^[9]

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

References

↑ Scotti PA, Urbanus ML, Brunner J, de Gier JW, von Heijne G, van der Does C, Driessen AJ, Oudega B, Luirink J. YidC, the Escherichia coli homologue of mitochondrial Oxa1p, is a component of the Sec translocase. EMBO J. 2000 Feb 15;19(4):542-9. PMID:10675323 doi:http://dx.doi.org/10.1093/emboj/19.4.542
↑ Samuelson JC, Chen M, Jiang F, Moller I, Wiedmann M, Kuhn A, Phillips GJ, Dalbey RE. YidC mediates membrane protein insertion in bacteria. Nature. 2000 Aug 10;406(6796):637-41. PMID:10949305 doi:http://dx.doi.org/10.1038/35020586
↑ van der Laan M, Urbanus ML, Ten Hagen-Jongman CM, Nouwen N, Oudega B, Harms N, Driessen AJ, Luirink J. A conserved function of YidC in the biogenesis of respiratory chain complexes. Proc Natl Acad Sci U S A. 2003 May 13;100(10):5801-6. Epub 2003 Apr 30. PMID:12724529 doi:http://dx.doi.org/10.1073/pnas.0636761100
↑ Yi L, Jiang F, Chen M, Cain B, Bolhuis A, Dalbey RE. YidC is strictly required for membrane insertion of subunits a and c of the F(1)F(0)ATP synthase and SecE of the SecYEG translocase. Biochemistry. 2003 Sep 9;42(35):10537-44. PMID:12950181 doi:http://dx.doi.org/10.1021/bi034309h
↑ Froderberg L, Houben EN, Baars L, Luirink J, de Gier JW. Targeting and translocation of two lipoproteins in Escherichia coli via the SRP/Sec/YidC pathway. J Biol Chem. 2004 Jul 23;279(30):31026-32. Epub 2004 May 12. PMID:15140892 doi:10.1074/jbc.M403229200
↑ Nagamori S, Smirnova IN, Kaback HR. Role of YidC in folding of polytopic membrane proteins. J Cell Biol. 2004 Apr;165(1):53-62. Epub 2004 Apr 5. PMID:15067017 doi:http://dx.doi.org/10.1083/jcb.200402067
↑ Xie K, Kiefer D, Nagler G, Dalbey RE, Kuhn A. Different regions of the nonconserved large periplasmic domain of Escherichia coli YidC are involved in the SecF interaction and membrane insertase activity. Biochemistry. 2006 Nov 7;45(44):13401-8. PMID:17073462 doi:http://dx.doi.org/10.1021/bi060826z
↑ Wagner S, Pop OI, Haan GJ, Baars L, Koningstein G, Klepsch MM, Genevaux P, Luirink J, de Gier JW. Biogenesis of MalF and the MalFGK(2) maltose transport complex in Escherichia coli requires YidC. J Biol Chem. 2008 Jun 27;283(26):17881-90. doi: 10.1074/jbc.M801481200. Epub 2008, May 2. PMID:18456666 doi:http://dx.doi.org/10.1074/jbc.M801481200
↑ Kedrov A, Wickles S, Crevenna AH, van der Sluis EO, Buschauer R, Berninghausen O, Lamb DC, Beckmann R. Structural Dynamics of the YidC:Ribosome Complex during Membrane Protein Biogenesis. Cell Rep. 2016 Dec 13;17(11):2943-2954. doi: 10.1016/j.celrep.2016.11.059. PMID:27974208 doi:http://dx.doi.org/10.1016/j.celrep.2016.11.059

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OCA

[1] Scotti PA, Urbanus ML, Brunner J, de Gier JW, von Heijne G, van der Does C, Driessen AJ, Oudega B, Luirink J. YidC, the Escherichia coli homologue of mitochondrial Oxa1p, is a component of the Sec translocase. EMBO J. 2000 Feb 15;19(4):542-9. PMID:10675323 doi:http://dx.doi.org/10.1093/emboj/19.4.542

[2] Samuelson JC, Chen M, Jiang F, Moller I, Wiedmann M, Kuhn A, Phillips GJ, Dalbey RE. YidC mediates membrane protein insertion in bacteria. Nature. 2000 Aug 10;406(6796):637-41. PMID:10949305 doi:http://dx.doi.org/10.1038/35020586

[3] van der Laan M, Urbanus ML, Ten Hagen-Jongman CM, Nouwen N, Oudega B, Harms N, Driessen AJ, Luirink J. A conserved function of YidC in the biogenesis of respiratory chain complexes. Proc Natl Acad Sci U S A. 2003 May 13;100(10):5801-6. Epub 2003 Apr 30. PMID:12724529 doi:http://dx.doi.org/10.1073/pnas.0636761100

[4] Yi L, Jiang F, Chen M, Cain B, Bolhuis A, Dalbey RE. YidC is strictly required for membrane insertion of subunits a and c of the F(1)F(0)ATP synthase and SecE of the SecYEG translocase. Biochemistry. 2003 Sep 9;42(35):10537-44. PMID:12950181 doi:http://dx.doi.org/10.1021/bi034309h

[5] Froderberg L, Houben EN, Baars L, Luirink J, de Gier JW. Targeting and translocation of two lipoproteins in Escherichia coli via the SRP/Sec/YidC pathway. J Biol Chem. 2004 Jul 23;279(30):31026-32. Epub 2004 May 12. PMID:15140892 doi:10.1074/jbc.M403229200

[6] Nagamori S, Smirnova IN, Kaback HR. Role of YidC in folding of polytopic membrane proteins. J Cell Biol. 2004 Apr;165(1):53-62. Epub 2004 Apr 5. PMID:15067017 doi:http://dx.doi.org/10.1083/jcb.200402067

[7] Xie K, Kiefer D, Nagler G, Dalbey RE, Kuhn A. Different regions of the nonconserved large periplasmic domain of Escherichia coli YidC are involved in the SecF interaction and membrane insertase activity. Biochemistry. 2006 Nov 7;45(44):13401-8. PMID:17073462 doi:http://dx.doi.org/10.1021/bi060826z

[8] Wagner S, Pop OI, Haan GJ, Baars L, Koningstein G, Klepsch MM, Genevaux P, Luirink J, de Gier JW. Biogenesis of MalF and the MalFGK(2) maltose transport complex in Escherichia coli requires YidC. J Biol Chem. 2008 Jun 27;283(26):17881-90. doi: 10.1074/jbc.M801481200. Epub 2008, May 2. PMID:18456666 doi:http://dx.doi.org/10.1074/jbc.M801481200

[9] Kedrov A, Wickles S, Crevenna AH, van der Sluis EO, Buschauer R, Berninghausen O, Lamb DC, Beckmann R. Structural Dynamics of the YidC:Ribosome Complex during Membrane Protein Biogenesis. Cell Rep. 2016 Dec 13;17(11):2943-2954. doi: 10.1016/j.celrep.2016.11.059. PMID:27974208 doi:http://dx.doi.org/10.1016/j.celrep.2016.11.059

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@@ Line 3: / Line 3: @@
 <SX load='5m5h' size='340' side='right' viewer='molstar' caption='[[5m5h]], [[Resolution|resolution]] 4.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5m5h]] is a 1 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=5M5H OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5M5H FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5m5h]] is a 1 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=5M5H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5M5H FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">yidC, ECS88_4129 ([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]] 4.5&#8491;</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=5m5h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m5h OCA], [http://pdbe.org/5m5h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5m5h RCSB], [http://www.ebi.ac.uk/pdbsum/5m5h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5m5h 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=5m5h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m5h OCA], [https://pdbe.org/5m5h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5m5h RCSB], [https://www.ebi.ac.uk/pdbsum/5m5h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5m5h ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/YIDC_ECO45 YIDC_ECO45]] Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins.
+[https://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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 25: / Line 25: @@
 __TOC__
 </SX>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
 [[Category: Large Structures]]
-[[Category: Beckmann, R]]
+[[Category: Beckmann R]]
-[[Category: Berninghausen, O]]
+[[Category: Berninghausen O]]
-[[Category: Buschauer, R]]
+[[Category: Buschauer R]]
-[[Category: Crevenna, A H]]
+[[Category: Crevenna AH]]
-[[Category: Kedrov, A]]
+[[Category: Kedrov A]]
-[[Category: Lamb, D C]]
+[[Category: Lamb DC]]
-[[Category: Sluis, E van der]]
+[[Category: Wickles S]]
-[[Category: Wickles, S]]
+[[Category: Van der Sluis E]]
-[[Category: Membrane protein]]
-[[Category: Nanodisc]]
-[[Category: Protein transport]]
-[[Category: Ribosome ligand]]

5m5h: Difference between revisions

Latest revision as of 21:26, 1 November 2023

RIBOSOME-BOUND YIDC INSERTASERIBOSOME-BOUND YIDC INSERTASE

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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5m5h: Difference between revisions

Latest revision as of 21:26, 1 November 2023

RIBOSOME-BOUND YIDC INSERTASERIBOSOME-BOUND YIDC INSERTASE

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

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