5jql: Difference between revisions

Revision as of 11:33, 17 June 2020

Crystal Structure of Phosphatidic acid Transporter Ups1/Mdm35 Void of Bound Phospholipid from Saccharomyces Cerevisiae at 2.9 Angstroms Resolution

Structural highlights

5jql is a 12 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:	MSE
Related:	5jqm, 5jqo
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[UPS1_YEAST] Required for maintenance of normal mitochondrial morphology as well as PCP1-dependent processing of MGM1. With UPS2, controls the level of cardiolipin in mitochondria. Cardiolipin is a unique phospholipid with four fatty acid chains and is present mainly in the mitochondrial inner membrane where it stabilizes the electron transport chain supercomplex between complexes III and IV through direct interaction of their subunits.^[1] ^[2] ^[3] ^[4] [MDM35_YEAST] Involved in mitochondrial distribution and morphology. Mediates the import of UPS1, UPS2 and UPS3, 3 atypical mitochondrial intermembrane space (IMS) proteins lacking the two major IMS-targeting signals, into the intermembrane space.^[5] ^[6] ^[7]

References

↑ Sesaki H, Dunn CD, Iijima M, Shepard KA, Yaffe MP, Machamer CE, Jensen RE. Ups1p, a conserved intermembrane space protein, regulates mitochondrial shape and alternative topogenesis of Mgm1p. J Cell Biol. 2006 Jun 5;173(5):651-8. PMID:16754953 doi:https://dx.doi.org/10.1083/jcb.200603092
↑ Osman C, Haag M, Potting C, Rodenfels J, Dip PV, Wieland FT, Brugger B, Westermann B, Langer T. The genetic interactome of prohibitins: coordinated control of cardiolipin and phosphatidylethanolamine by conserved regulators in mitochondria. J Cell Biol. 2009 Feb 23;184(4):583-96. doi: 10.1083/jcb.200810189. Epub 2009 Feb, 16. PMID:19221197 doi:https://dx.doi.org/10.1083/jcb.200810189
↑ Tamura Y, Endo T, Iijima M, Sesaki H. Ups1p and Ups2p antagonistically regulate cardiolipin metabolism in mitochondria. J Cell Biol. 2009 Jun 15;185(6):1029-45. Epub 2009 Jun 8. PMID:19506038 doi:https://dx.doi.org/jcb.200812018
↑ Tamura Y, Iijima M, Sesaki H. Mdm35p imports Ups proteins into the mitochondrial intermembrane space by functional complex formation. EMBO J. 2010 Sep 1;29(17):2875-87. doi: 10.1038/emboj.2010.149. Epub 2010 Jul 9. PMID:20622808 doi:https://dx.doi.org/10.1038/emboj.2010.149
↑ Dimmer KS, Fritz S, Fuchs F, Messerschmitt M, Weinbach N, Neupert W, Westermann B. Genetic basis of mitochondrial function and morphology in Saccharomyces cerevisiae. Mol Biol Cell. 2002 Mar;13(3):847-53. PMID:11907266 doi:10.1091/mbc.01-12-0588
↑ Tamura Y, Iijima M, Sesaki H. Mdm35p imports Ups proteins into the mitochondrial intermembrane space by functional complex formation. EMBO J. 2010 Sep 1;29(17):2875-87. doi: 10.1038/emboj.2010.149. Epub 2010 Jul 9. PMID:20622808 doi:https://dx.doi.org/10.1038/emboj.2010.149
↑ Potting C, Wilmes C, Engmann T, Osman C, Langer T. Regulation of mitochondrial phospholipids by Ups1/PRELI-like proteins depends on proteolysis and Mdm35. EMBO J. 2010 Sep 1;29(17):2888-98. doi: 10.1038/emboj.2010.169. Epub 2010 Jul 23. PMID:20657548 doi:https://dx.doi.org/10.1038/emboj.2010.169

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Sesaki H, Dunn CD, Iijima M, Shepard KA, Yaffe MP, Machamer CE, Jensen RE. Ups1p, a conserved intermembrane space protein, regulates mitochondrial shape and alternative topogenesis of Mgm1p. J Cell Biol. 2006 Jun 5;173(5):651-8. PMID:16754953 doi:https://dx.doi.org/10.1083/jcb.200603092

[2] Osman C, Haag M, Potting C, Rodenfels J, Dip PV, Wieland FT, Brugger B, Westermann B, Langer T. The genetic interactome of prohibitins: coordinated control of cardiolipin and phosphatidylethanolamine by conserved regulators in mitochondria. J Cell Biol. 2009 Feb 23;184(4):583-96. doi: 10.1083/jcb.200810189. Epub 2009 Feb, 16. PMID:19221197 doi:https://dx.doi.org/10.1083/jcb.200810189

[3] Tamura Y, Endo T, Iijima M, Sesaki H. Ups1p and Ups2p antagonistically regulate cardiolipin metabolism in mitochondria. J Cell Biol. 2009 Jun 15;185(6):1029-45. Epub 2009 Jun 8. PMID:19506038 doi:https://dx.doi.org/jcb.200812018

[4] Tamura Y, Iijima M, Sesaki H. Mdm35p imports Ups proteins into the mitochondrial intermembrane space by functional complex formation. EMBO J. 2010 Sep 1;29(17):2875-87. doi: 10.1038/emboj.2010.149. Epub 2010 Jul 9. PMID:20622808 doi:https://dx.doi.org/10.1038/emboj.2010.149

[5] Dimmer KS, Fritz S, Fuchs F, Messerschmitt M, Weinbach N, Neupert W, Westermann B. Genetic basis of mitochondrial function and morphology in Saccharomyces cerevisiae. Mol Biol Cell. 2002 Mar;13(3):847-53. PMID:11907266 doi:10.1091/mbc.01-12-0588

[6] Tamura Y, Iijima M, Sesaki H. Mdm35p imports Ups proteins into the mitochondrial intermembrane space by functional complex formation. EMBO J. 2010 Sep 1;29(17):2875-87. doi: 10.1038/emboj.2010.149. Epub 2010 Jul 9. PMID:20622808 doi:https://dx.doi.org/10.1038/emboj.2010.149

[7] Potting C, Wilmes C, Engmann T, Osman C, Langer T. Regulation of mitochondrial phospholipids by Ups1/PRELI-like proteins depends on proteolysis and Mdm35. EMBO J. 2010 Sep 1;29(17):2888-98. doi: 10.1038/emboj.2010.169. Epub 2010 Jul 23. PMID:20657548 doi:https://dx.doi.org/10.1038/emboj.2010.169

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@@ Line 1: / Line 1: @@
 ==Crystal Structure of Phosphatidic acid Transporter Ups1/Mdm35 Void of Bound Phospholipid from Saccharomyces Cerevisiae at 2.9 Angstroms Resolution==
-<StructureSection load='5jql' size='340' side='right' caption='[[5jql]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
+<StructureSection load='5jql' size='340' side='right'caption='[[5jql]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5jql]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JQL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JQL FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5jql]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JQL OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5JQL FirstGlance]. <br>
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5jqm|5jqm]], [[5jqo|5jqo]]</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=5jql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jql OCA], [http://pdbe.org/5jql PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jql RCSB], [http://www.ebi.ac.uk/pdbsum/5jql PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jql 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=5jql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jql OCA], [http://pdbe.org/5jql PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jql RCSB], [http://www.ebi.ac.uk/pdbsum/5jql PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jql ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 14: @@
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Chan, K C]]
 [[Category: Fan, J]]

5jql: Difference between revisions

Revision as of 11:33, 17 June 2020

Crystal Structure of Phosphatidic acid Transporter Ups1/Mdm35 Void of Bound Phospholipid from Saccharomyces Cerevisiae at 2.9 Angstroms Resolution

Structural highlights

Function

References

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