6d71: Difference between revisions
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<StructureSection load='6d71' size='340' side='right'caption='[[6d71]], [[Resolution|resolution]] 1.72Å' scene=''> | <StructureSection load='6d71' size='340' side='right'caption='[[6d71]], [[Resolution|resolution]] 1.72Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6d71]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6d71]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6D71 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6D71 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7180779Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6d71 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6d71 OCA], [https://pdbe.org/6d71 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6d71 RCSB], [https://www.ebi.ac.uk/pdbsum/6d71 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6d71 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/MIRO1_HUMAN MIRO1_HUMAN] Mitochondrial GTPase involved in mitochondrial trafficking. Probably involved in control of anterograde transport of mitochondria and their subcellular distribution.<ref>PMID:12482879</ref> <ref>PMID:16630562</ref> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Dysfunction in mitochondrial dynamics is believed to contribute to a host of neurological disorders and has recently been implicated in cancer metastasis. The outer mitochondrial membrane adapter protein Miro functions in the regulation of mitochondrial mobility and degradation, however, the structural basis for its roles in mitochondrial regulation remain unknown. Here, we report a 1.7A crystal structure of N-terminal GTPase domain (nGTPase) of human Miro1 bound unexpectedly to GTP, thereby revealing a non-catalytic configuration of the putative GTPase active site. We identify two conserved surfaces of the nGTPase, the "SELFYY" and "ITIP" motifs, that are potentially positioned to mediate dimerization or interaction with binding partners. Additionally, we report small angle X-ray scattering (SAXS) data obtained from the intact soluble HsMiro1 and its paralog HsMiro2. Taken together, the data allow modeling of a crescent-shaped assembly of the soluble domain of HsMiro1/2. PDB RSEFERENCE: Crystal structure of the human Miro1 N-terminal GTPase bound to GTP, 6D71. | |||
Insight into human Miro1/2 domain organization based on the structure of its N-terminal GTPase.,Smith KP, Focia PJ, Chakravarthy S, Landahl EC, Klosowiak JL, Rice SE, Freymann DM J Struct Biol. 2020 Oct 24;212(3):107656. doi: 10.1016/j.jsb.2020.107656. PMID:33132189<ref>PMID:33132189</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6d71" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[GTP-binding protein 3D structures|GTP-binding protein 3D structures]] | |||
*[[Rho GTPase 3D structures|Rho GTPase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Focia | [[Category: Focia PJ]] | ||
[[Category: Freymann | [[Category: Freymann DM]] | ||
[[Category: Rice | [[Category: Rice SE]] | ||
[[Category: Smith | [[Category: Smith KP]] | ||
Latest revision as of 13:07, 22 May 2024
Crystal Structure of the Human Miro1 N-terminal GTPase bound to GTPCrystal Structure of the Human Miro1 N-terminal GTPase bound to GTP
Structural highlights
FunctionMIRO1_HUMAN Mitochondrial GTPase involved in mitochondrial trafficking. Probably involved in control of anterograde transport of mitochondria and their subcellular distribution.[1] [2] Publication Abstract from PubMedDysfunction in mitochondrial dynamics is believed to contribute to a host of neurological disorders and has recently been implicated in cancer metastasis. The outer mitochondrial membrane adapter protein Miro functions in the regulation of mitochondrial mobility and degradation, however, the structural basis for its roles in mitochondrial regulation remain unknown. Here, we report a 1.7A crystal structure of N-terminal GTPase domain (nGTPase) of human Miro1 bound unexpectedly to GTP, thereby revealing a non-catalytic configuration of the putative GTPase active site. We identify two conserved surfaces of the nGTPase, the "SELFYY" and "ITIP" motifs, that are potentially positioned to mediate dimerization or interaction with binding partners. Additionally, we report small angle X-ray scattering (SAXS) data obtained from the intact soluble HsMiro1 and its paralog HsMiro2. Taken together, the data allow modeling of a crescent-shaped assembly of the soluble domain of HsMiro1/2. PDB RSEFERENCE: Crystal structure of the human Miro1 N-terminal GTPase bound to GTP, 6D71. Insight into human Miro1/2 domain organization based on the structure of its N-terminal GTPase.,Smith KP, Focia PJ, Chakravarthy S, Landahl EC, Klosowiak JL, Rice SE, Freymann DM J Struct Biol. 2020 Oct 24;212(3):107656. doi: 10.1016/j.jsb.2020.107656. PMID:33132189[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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