3ggz

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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==
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<StructureSection load='3ggz' size='340' side='right' caption='[[3ggz]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
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<StructureSection load='3ggz' size='340' side='right'caption='[[3ggz]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<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>
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<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>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ggy|3ggy]]</td></tr>
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</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>
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<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>
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<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>
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<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>
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<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 ==
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[[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>
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[[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>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gg/3ggz_consurf.spt"</scriptWhenChecked>
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<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>
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==See Also==
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*[[Increased sodium tolerance protein|Increased sodium tolerance protein]]
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*[[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]]
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[[Category: Large Structures]]
[[Category: Xiao, J]]
[[Category: Xiao, J]]
[[Category: Xu, Z]]
[[Category: Xu, Z]]

Revision as of 08:05, 9 March 2022

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

PDB ID 3ggz

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