2xu6

From Proteopedia

(Difference between revisions)

Revision as of 12:17, 27 April 2022

MDV1 coiled coil domain

Structural highlights

2xu6 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.
NonStd Res:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MDV1_YEAST] Involved in mitochondrial fission. Has a partially redundant function to CAF4 in acting as an adapter protein, binding to FIS1 on the mitochondrial outer membrane and recruiting the dynamin-like GTPase DNM1 to form mitochondrial fission complexes. Formation of these complexes is required to promote constriction and fission of the mitochondrial compartment at a late step in mitochondrial division.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7]

Publication Abstract from PubMed

Recruitment and assembly of some dynamin-related guanosine triphosphatases depends on adaptor proteins restricted to distinct cellular membranes. The yeast Mdv1 adaptor localizes to mitochondria by binding to the membrane protein Fis1. Subsequent Mdv1 binding to the mitochondrial dynamin Dnm1 stimulates Dnm1 assembly into spirals, which encircle and divide the mitochondrial compartment. In this study, we report that dimeric Mdv1 is joined at its center by a 92-A antiparallel coiled coil (CC). Modeling of the Fis1-Mdv1 complex using available crystal structures suggests that the Mdv1 CC lies parallel to the bilayer with N termini at opposite ends bound to Fis1 and C-terminal beta-propeller domains (Dnm1-binding sites) extending into the cytoplasm. A CC length of appropriate length and sequence is necessary for optimal Mdv1 interaction with Fis1 and Dnm1 and is important for proper Dnm1 assembly before membrane scission. Our results provide a framework for understanding how adaptors act as scaffolds to orient and stabilize the assembly of dynamins on membranes.

Molecular architecture of a dynamin adaptor: implications for assembly of mitochondrial fission complexes.,Koirala S, Bui HT, Schubert HL, Eckert DM, Hill CP, Kay MS, Shaw JM J Cell Biol. 2010 Dec 13;191(6):1127-39. PMID:21149566^[8]

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

References

↑ Tieu Q, Nunnari J. Mdv1p is a WD repeat protein that interacts with the dynamin-related GTPase, Dnm1p, to trigger mitochondrial division. J Cell Biol. 2000 Oct 16;151(2):353-66. PMID:11038182
↑ Fekkes P, Shepard KA, Yaffe MP. Gag3p, an outer membrane protein required for fission of mitochondrial tubules. J Cell Biol. 2000 Oct 16;151(2):333-40. PMID:11038180
↑ Mozdy AD, McCaffery JM, Shaw JM. Dnm1p GTPase-mediated mitochondrial fission is a multi-step process requiring the novel integral membrane component Fis1p. J Cell Biol. 2000 Oct 16;151(2):367-80. PMID:11038183
↑ Tieu Q, Okreglak V, Naylor K, Nunnari J. The WD repeat protein, Mdv1p, functions as a molecular adaptor by interacting with Dnm1p and Fis1p during mitochondrial fission. J Cell Biol. 2002 Aug 5;158(3):445-52. Epub 2002 Aug 5. PMID:12163467 doi:http://dx.doi.org/10.1083/jcb.200205031
↑ Karren MA, Coonrod EM, Anderson TK, Shaw JM. The role of Fis1p-Mdv1p interactions in mitochondrial fission complex assembly. J Cell Biol. 2005 Oct 24;171(2):291-301. PMID:16247028 doi:http://dx.doi.org/10.1083/jcb.200506158
↑ Naylor K, Ingerman E, Okreglak V, Marino M, Hinshaw JE, Nunnari J. Mdv1 interacts with assembled dnm1 to promote mitochondrial division. J Biol Chem. 2006 Jan 27;281(4):2177-83. Epub 2005 Nov 4. PMID:16272155 doi:http://dx.doi.org/10.1074/jbc.M507943200
↑ Bhar D, Karren MA, Babst M, Shaw JM. Dimeric Dnm1-G385D interacts with Mdv1 on mitochondria and can be stimulated to assemble into fission complexes containing Mdv1 and Fis1. J Biol Chem. 2006 Jun 23;281(25):17312-20. Epub 2006 Apr 6. PMID:16601120 doi:http://dx.doi.org/10.1074/jbc.M513530200
↑ Koirala S, Bui HT, Schubert HL, Eckert DM, Hill CP, Kay MS, Shaw JM. Molecular architecture of a dynamin adaptor: implications for assembly of mitochondrial fission complexes. J Cell Biol. 2010 Dec 13;191(6):1127-39. PMID:21149566 doi:10.1083/jcb.201005046

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/2xu6"

@@ Line 3: / Line 3: @@
 <StructureSection load='2xu6' size='340' side='right'caption='[[2xu6]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2xu6]] is a 2 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=2XU6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2XU6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2xu6]] is a 2 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=2XU6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XU6 FirstGlance]. <br>
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2xu6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xu6 OCA], [http://pdbe.org/2xu6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xu6 RCSB], [http://www.ebi.ac.uk/pdbsum/2xu6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xu6 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=2xu6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xu6 OCA], [https://pdbe.org/2xu6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xu6 RCSB], [https://www.ebi.ac.uk/pdbsum/2xu6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xu6 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/MDV1_YEAST MDV1_YEAST]] Involved in mitochondrial fission. Has a partially redundant function to CAF4 in acting as an adapter protein, binding to FIS1 on the mitochondrial outer membrane and recruiting the dynamin-like GTPase DNM1 to form mitochondrial fission complexes. Formation of these complexes is required to promote constriction and fission of the mitochondrial compartment at a late step in mitochondrial division.<ref>PMID:11038182</ref> <ref>PMID:11038180</ref> <ref>PMID:11038183</ref> <ref>PMID:12163467</ref> <ref>PMID:16247028</ref> <ref>PMID:16272155</ref> <ref>PMID:16601120</ref>
+[[https://www.uniprot.org/uniprot/MDV1_YEAST MDV1_YEAST]] Involved in mitochondrial fission. Has a partially redundant function to CAF4 in acting as an adapter protein, binding to FIS1 on the mitochondrial outer membrane and recruiting the dynamin-like GTPase DNM1 to form mitochondrial fission complexes. Formation of these complexes is required to promote constriction and fission of the mitochondrial compartment at a late step in mitochondrial division.<ref>PMID:11038182</ref> <ref>PMID:11038180</ref> <ref>PMID:11038183</ref> <ref>PMID:12163467</ref> <ref>PMID:16247028</ref> <ref>PMID:16272155</ref> <ref>PMID:16601120</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

2xu6

From Proteopedia

Revision as of 12:17, 27 April 2022

MDV1 coiled coil domain

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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