This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

4txp

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 01:13, 19 January 2017

Crystal structure of LIP5 N-terminal domain

Structural highlights

4txp is a 3 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	4txq, 4txr
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[VTA1_HUMAN] Involved in the endosomal multivesicular bodies (MVB) pathway. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. Thought to be a cofactor of VPS4A/B, which catalyzes disassembles membrane-associated ESCRT-III assemblies. Involved in the sorting and down-regulation of EGFR (By similarity). Involved in HIV-1 budding.^[1]

Publication Abstract from PubMed

Disassembly of the endosomal sorting complex required for transport (ESCRT) machinery from biological membranes is a critical final step in cellular processes that require the ESCRT function. This reaction is catalyzed by VPS4, a AAA-ATPase whose activity is tightly regulated by a host of proteins including LIP5 and the ESCRT-III proteins. Here, we present structural and functional analyses of molecular interactions between human VPS4, LIP5 and the ESCRT-III proteins. The N-terminal domain of LIP5 (LIP5NTD) is required for LIP5-mediated stimulation of VPS4 and the ESCRT-III protein CHMP5 strongly inhibits the stimulation. Both of these observations are distinct from what was previously described for homologous yeast proteins. The crystal structure of LIP5NTD in complex with the MIT-interacting motifs (MIMs) of CHMP5 and a second ESCRT-III protein CHMP1B was determined at 1 angstrom resolution. It reveals an ESCRT-III binding induced moderate conformational change in LIP5NTD, which results from insertion of a conserved CHMP5 tyrosine residue (Tyr182) at the core of LIP5NTD structure. Mutation of Tyr182 partially relieves the inhibition displayed by CHMP5. Together, these results suggest a novel mechanism of VPS4 regulation in metazoans, where CHMP5 functions as a negative allosteric switch to control LIP5-mediated stimulation of VPS4.

A Novel Mechanism of Regulating the ATPase VPS4 by Its Cofactor LIP5 and the Endosomal Sorting Complex Required for Transport (ESCRT)-III Protein CHMP5.,Vild CJ, Li Y, Guo EZ, Liu Y, Xu Z J Biol Chem. 2015 Jan 30. pii: jbc.M114.616730. PMID:25637630^[2]

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

References

↑ Ward DM, Vaughn MB, Shiflett SL, White PL, Pollock AL, Hill J, Schnegelberger R, Sundquist WI, Kaplan J. The role of LIP5 and CHMP5 in multivesicular body formation and HIV-1 budding in mammalian cells. J Biol Chem. 2005 Mar 18;280(11):10548-55. Epub 2005 Jan 11. PMID:15644320 doi:http://dx.doi.org/M413734200
↑ Vild CJ, Li Y, Guo EZ, Liu Y, Xu Z. A Novel Mechanism of Regulating the ATPase VPS4 by Its Cofactor LIP5 and the Endosomal Sorting Complex Required for Transport (ESCRT)-III Protein CHMP5. J Biol Chem. 2015 Jan 30. pii: jbc.M114.616730. PMID:25637630 doi:http://dx.doi.org/10.1074/jbc.M114.616730

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4txp"

@@ Line 1: / Line 1: @@
 ==Crystal structure of LIP5 N-terminal domain==
 <StructureSection load='4txp' size='340' side='right' caption='[[4txp]], [[Resolution|resolution]] 3.01&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[4txp]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TXP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TXP FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4txq|4txq]], [[4txr|4txr]]</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=4txp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4txp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4txp RCSB], [http://www.ebi.ac.uk/pdbsum/4txp 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=4txp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4txp OCA], [http://pdbe.org/4txp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4txp RCSB], [http://www.ebi.ac.uk/pdbsum/4txp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4txp ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 16: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4txp" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4txp

From Proteopedia

Revision as of 01:13, 19 January 2017

Crystal structure of LIP5 N-terminal domain

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox