4oah

From Proteopedia

(Difference between revisions)

Revision as of 12:15, 4 August 2016

Crystal structure of the cytosolic domain of mouse MiD51 H201A mutant

Structural highlights

4oah is a 4 chain structure with sequence from Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	4oaf, 4oag, 4oai
Gene:	Mid51, MiD51 (aka SMCR7L), Mief1, Smcr7l (LK3 transgenic mice)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MID51_MOUSE] Mitochondrial outer membrane protein which regulates mitochondrial fission. Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface independently of the mitochondrial fission FIS1 and MFF proteins.

Publication Abstract from PubMed

Mitochondrial fission requires recruitment of dynamin-related protein 1 (Drp1) to the mitochondrial surface and activation of its GTP-dependent scission function. The Drp1 receptors MiD49 and MiD51 recruit Drp1 to facilitate mitochondrial fission, but their mechanism of action is poorly understood. Using X-ray crystallography, we demonstrate that MiD51 contains a nucleotidyl transferase domain that binds ADP with high affinity. MiD51 recruits Drp1 via a surface loop that functions independently of ADP binding. However, in the absence of nucleotide binding, the recruited Drp1 cannot be activated for fission. Purified MiD51 strongly inhibits Drp1 assembly and GTP hydrolysis in the absence of ADP. Addition of ADP relieves this inhibition and promotes Drp1 assembly into spirals with enhanced GTP hydrolysis. Our results reveal ADP as an essential cofactor for MiD51 during mitochondrial fission.

The Mitochondrial Fission Receptor MiD51 Requires ADP as a Cofactor.,Loson OC, Liu R, Rome ME, Meng S, Kaiser JT, Shan SO, Chan DC Structure. 2014 Mar 4;22(3):367-77. doi: 10.1016/j.str.2014.01.001. Epub 2014 Feb, 6. PMID:24508339^[1]

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

References

↑ Loson OC, Liu R, Rome ME, Meng S, Kaiser JT, Shan SO, Chan DC. The Mitochondrial Fission Receptor MiD51 Requires ADP as a Cofactor. Structure. 2014 Mar 4;22(3):367-77. doi: 10.1016/j.str.2014.01.001. Epub 2014 Feb, 6. PMID:24508339 doi:http://dx.doi.org/10.1016/j.str.2014.01.001

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/4oah"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the cytosolic domain of mouse MiD51 H201A mutant==
 <StructureSection load='4oah' size='340' side='right' caption='[[4oah]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4oaf|4oaf]], [[4oag|4oag]], [[4oai|4oai]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Mid51, MiD51 (aka SMCR7L), Mief1, Smcr7l ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=4oah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oah OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oah RCSB], [http://www.ebi.ac.uk/pdbsum/4oah 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=4oah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oah OCA], [http://pdbe.org/4oah PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4oah RCSB], [http://www.ebi.ac.uk/pdbsum/4oah PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4oah ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4oah" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4oah

From Proteopedia

Revision as of 12:15, 4 August 2016

Crystal structure of the cytosolic domain of mouse MiD51 H201A mutant

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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