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| ==Crystal Structure of S.cerevisiae Ist1 N-terminal domain in complex with Did2 MIM motif== | | ==Crystal Structure of S.cerevisiae Ist1 N-terminal domain in complex with Did2 MIM motif== |
- | <StructureSection load='3ggz' size='340' side='right' caption='[[3ggz]], [[Resolution|resolution]] 3.80Å' scene=''> | + | <StructureSection load='3ggz' size='340' side='right'caption='[[3ggz]], [[Resolution|resolution]] 3.80Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[3ggz]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GGZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3GGZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ggz]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GGZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GGZ FirstGlance]. <br> |
- | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ggy|3ggy]]</td></tr> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ggy|3ggy]]</div></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IST1, N0809, YNL265C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), CHM1, DID2, FTI1, VPS46, YKR035W-A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IST1, N0809, YNL265C ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), CHM1, DID2, FTI1, VPS46, YKR035W-A ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=3ggz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ggz OCA], [http://pdbe.org/3ggz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ggz RCSB], [http://www.ebi.ac.uk/pdbsum/3ggz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ggz 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=3ggz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ggz OCA], [https://pdbe.org/3ggz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ggz RCSB], [https://www.ebi.ac.uk/pdbsum/3ggz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ggz ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/IST1_YEAST IST1_YEAST]] Involved in a late step in sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles. The lumenal sequestrated membrane proteins are targeted into the vacuole after fusion of the endosome with the vacuole. Regulates the recruitment of VPS4 to the ESCRT-III complex, probably in conjunction with DID2, and VPS4 catalyzes the disassembly of the ESCRT-III complex.<ref>PMID:18032582</ref> <ref>PMID:18032584</ref> [[http://www.uniprot.org/uniprot/DID2_YEAST DID2_YEAST]] Class E VPS protein implicated in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles. The lumenal sequestrated membrane proteins will be targeted into the vacuole after fusion of the endosome with the vacuole. Probably acts as a peripherally associated component of the ESCRT-III complex, which appears to be critical for late steps in MVB sorting, such as membrane invagination and final cargo sorting and recruits late-acting components of the sorting machinery. The MVB pathway requires the sequential function of ESCRT-O, -I,-II and -III complex assemblies. Regulates the membrane association of VPS4. Can stimulate VPS4 ATPase activity directly or via VTA1.<ref>PMID:11029042</ref> <ref>PMID:11559748</ref> <ref>PMID:15086794</ref> <ref>PMID:16601096</ref> <ref>PMID:17130288</ref> <ref>PMID:18032584</ref> <ref>PMID:18194652</ref> | + | [[https://www.uniprot.org/uniprot/IST1_YEAST IST1_YEAST]] Involved in a late step in sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles. The lumenal sequestrated membrane proteins are targeted into the vacuole after fusion of the endosome with the vacuole. Regulates the recruitment of VPS4 to the ESCRT-III complex, probably in conjunction with DID2, and VPS4 catalyzes the disassembly of the ESCRT-III complex.<ref>PMID:18032582</ref> <ref>PMID:18032584</ref> [[https://www.uniprot.org/uniprot/DID2_YEAST DID2_YEAST]] Class E VPS protein implicated in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles. The lumenal sequestrated membrane proteins will be targeted into the vacuole after fusion of the endosome with the vacuole. Probably acts as a peripherally associated component of the ESCRT-III complex, which appears to be critical for late steps in MVB sorting, such as membrane invagination and final cargo sorting and recruits late-acting components of the sorting machinery. The MVB pathway requires the sequential function of ESCRT-O, -I,-II and -III complex assemblies. Regulates the membrane association of VPS4. Can stimulate VPS4 ATPase activity directly or via VTA1.<ref>PMID:11029042</ref> <ref>PMID:11559748</ref> <ref>PMID:15086794</ref> <ref>PMID:16601096</ref> <ref>PMID:17130288</ref> <ref>PMID:18032584</ref> <ref>PMID:18194652</ref> |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Check<jmol> | | Check<jmol> |
| <jmolCheckbox> | | <jmolCheckbox> |
- | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gg/3ggz_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gg/3ggz_consurf.spt"</scriptWhenChecked> |
| <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
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| </div> | | </div> |
| <div class="pdbe-citations 3ggz" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 3ggz" style="background-color:#fffaf0;"></div> |
| + | |
| + | ==See Also== |
| + | *[[Increased sodium tolerance protein|Increased sodium tolerance protein]] |
| + | *[[Vacuolar protein sorting-associated protein 3D structures|Vacuolar protein sorting-associated protein 3D structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
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| </StructureSection> | | </StructureSection> |
| [[Category: Atcc 18824]] | | [[Category: Atcc 18824]] |
| + | [[Category: Large Structures]] |
| [[Category: Xiao, J]] | | [[Category: Xiao, J]] |
| [[Category: Xu, Z]] | | [[Category: Xu, Z]] |
| Structural highlights
3ggz is a 8 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| Related: | |
Gene: | IST1, N0809, YNL265C (ATCC 18824), CHM1, DID2, FTI1, VPS46, YKR035W-A (ATCC 18824) |
Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[IST1_YEAST] Involved in a late step in sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles. The lumenal sequestrated membrane proteins are targeted into the vacuole after fusion of the endosome with the vacuole. Regulates the recruitment of VPS4 to the ESCRT-III complex, probably in conjunction with DID2, and VPS4 catalyzes the disassembly of the ESCRT-III complex.[1] [2] [DID2_YEAST] Class E VPS protein implicated in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles. The lumenal sequestrated membrane proteins will be targeted into the vacuole after fusion of the endosome with the vacuole. Probably acts as a peripherally associated component of the ESCRT-III complex, which appears to be critical for late steps in MVB sorting, such as membrane invagination and final cargo sorting and recruits late-acting components of the sorting machinery. The MVB pathway requires the sequential function of ESCRT-O, -I,-II and -III complex assemblies. Regulates the membrane association of VPS4. Can stimulate VPS4 ATPase activity directly or via VTA1.[3] [4] [5] [6] [7] [8] [9]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The ESCRT machinery functions in several important eukaryotic cellular processes. The AAA-ATPase Vps4 catalyzes disassembly of the ESCRT-III complex and may regulate membrane deformation and vesicle scission as well. Ist1 was proposed to be a regulator of Vps4, but its mechanism of action was unclear. The crystal structure of the N-terminal domain of Ist1 (Ist1NTD) reveals an ESCRT-III subunit-like fold, implicating Ist1 as a divergent ESCRT-III family member. Ist1NTD specifically binds to the ESCRT-III subunit Did2, and cocrystallization of Ist1NTD with a Did2 fragment shows that Ist1 interacts with the Did2 C-terminal MIM1 (MIT-interacting motif 1) via a novel MIM-binding structural motif. This arrangement indicates a mechanism for intermolecular ESCRT-III subunit association and may also suggest one form of ESCRT-III subunit autoinhibition via intramolecular interaction.
Structural basis of Ist1 function and Ist1-Did2 interaction in the multivesicular body pathway and cytokinesis.,Xiao J, Chen XW, Davies BA, Saltiel AR, Katzmann DJ, Xu Z Mol Biol Cell. 2009 Aug;20(15):3514-24. Epub 2009 May 28. PMID:19477918[10]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Dimaano C, Jones CB, Hanono A, Curtiss M, Babst M. Ist1 regulates Vps4 localization and assembly. Mol Biol Cell. 2008 Feb;19(2):465-74. Epub 2007 Nov 21. PMID:18032582 doi:http://dx.doi.org/E07-08-0747
- ↑ Rue SM, Mattei S, Saksena S, Emr SD. Novel Ist1-Did2 complex functions at a late step in multivesicular body sorting. Mol Biol Cell. 2008 Feb;19(2):475-84. Epub 2007 Nov 21. PMID:18032584 doi:http://dx.doi.org/E07-07-0694
- ↑ Amerik AY, Nowak J, Swaminathan S, Hochstrasser M. The Doa4 deubiquitinating enzyme is functionally linked to the vacuolar protein-sorting and endocytic pathways. Mol Biol Cell. 2000 Oct;11(10):3365-80. PMID:11029042
- ↑ Howard TL, Stauffer DR, Degnin CR, Hollenberg SM. CHMP1 functions as a member of a newly defined family of vesicle trafficking proteins. J Cell Sci. 2001 Jul;114(Pt 13):2395-404. PMID:11559748
- ↑ Bowers K, Lottridge J, Helliwell SB, Goldthwaite LM, Luzio JP, Stevens TH. Protein-protein interactions of ESCRT complexes in the yeast Saccharomyces cerevisiae. Traffic. 2004 Mar;5(3):194-210. PMID:15086794 doi:10.1111/j.1600-0854.2004.00169.x
- ↑ Lottridge JM, Flannery AR, Vincelli JL, Stevens TH. Vta1p and Vps46p regulate the membrane association and ATPase activity of Vps4p at the yeast multivesicular body. Proc Natl Acad Sci U S A. 2006 Apr 18;103(16):6202-7. Epub 2006 Apr 6. PMID:16601096 doi:0601712103
- ↑ Nickerson DP, West M, Odorizzi G. Did2 coordinates Vps4-mediated dissociation of ESCRT-III from endosomes. J Cell Biol. 2006 Dec 4;175(5):715-20. Epub 2006 Nov 27. PMID:17130288 doi:http://dx.doi.org/jcb.200606113
- ↑ Rue SM, Mattei S, Saksena S, Emr SD. Novel Ist1-Did2 complex functions at a late step in multivesicular body sorting. Mol Biol Cell. 2008 Feb;19(2):475-84. Epub 2007 Nov 21. PMID:18032584 doi:http://dx.doi.org/E07-07-0694
- ↑ Azmi IF, Davies BA, Xiao J, Babst M, Xu Z, Katzmann DJ. ESCRT-III family members stimulate Vps4 ATPase activity directly or via Vta1. Dev Cell. 2008 Jan;14(1):50-61. PMID:18194652 doi:http://dx.doi.org/S1534-5807(07)00432-7
- ↑ Xiao J, Chen XW, Davies BA, Saltiel AR, Katzmann DJ, Xu Z. Structural basis of Ist1 function and Ist1-Did2 interaction in the multivesicular body pathway and cytokinesis. Mol Biol Cell. 2009 Aug;20(15):3514-24. Epub 2009 May 28. PMID:19477918 doi:10.1091/mbc.E09-05-0403
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