3ggz: Difference between revisions

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<StructureSection load='3ggz' size='340' side='right'caption='[[3ggz]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
<StructureSection load='3ggz' size='340' side='right'caption='[[3ggz]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<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>
<table><tr><td colspan='2'>[[3ggz]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. 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"><div style='overflow: auto; max-height: 3em;'>[[3ggy|3ggy]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.8&#8491;</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'>[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>
<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 ==
[[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> 
[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>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3ggz ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3ggz ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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<ref>PMID:19477918</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3ggz" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 18824]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Xiao, J]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Xu, Z]]
[[Category: Xiao J]]
[[Category: Coiled coil]]
[[Category: Xu Z]]
[[Category: Endocytosis]]
[[Category: Endosome]]
[[Category: Membrane]]
[[Category: Novel mim binding mode]]
[[Category: Phosphoprotein]]
[[Category: Protein transport]]
[[Category: Transport]]

Latest revision as of 09:54, 21 February 2024

Crystal Structure of S.cerevisiae Ist1 N-terminal domain in complex with Did2 MIM motif

3ggz, resolution 3.80Å

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