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3ggy

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Revision as of 07:05, 1 November 2017

Crystal Structure of S.cerevisiae Ist1 N-terminal domain

Structural highlights

3ggy is a 2 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:	3ggz
Gene:	IST1, N0809, YNL265C (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]

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^[3]

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

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
↑ 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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3ggy"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of S.cerevisiae Ist1 N-terminal domain==
 <StructureSection load='3ggy' size='340' side='right' caption='[[3ggy]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ggz|3ggz]]</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])</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=3ggy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ggy OCA], [http://pdbe.org/3ggy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ggy RCSB], [http://www.ebi.ac.uk/pdbsum/3ggy PDBsum]</span></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=3ggy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ggy OCA], [http://pdbe.org/3ggy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ggy RCSB], [http://www.ebi.ac.uk/pdbsum/3ggy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ggy ProSAT]</span></td></tr>
 </table>
 == Function ==

3ggy

From Proteopedia

Revision as of 07:05, 1 November 2017

Crystal Structure of S.cerevisiae Ist1 N-terminal domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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