5h5a

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'''Unreleased structure'''
 
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The entry 5h5a is ON HOLD until Paper Publication
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==Mdm12 from K. lactis (1-239), Lys residues are uniformly dimethyl modified==
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<StructureSection load='5h5a' size='340' side='right' caption='[[5h5a]], [[Resolution|resolution]] 2.26&Aring;' scene=''>
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Authors: Kawano, S., Quinbara, S., Endo, T.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5h5a]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H5A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5H5A FirstGlance]. <br>
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Description: Mdm12 from K. lactis (1-239), Lys residues are uniformly dimethyl modified
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6OU:[(2~{R})-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-yl]+(~{Z})-octadec-9-enoate'>6OU</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
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[[Category: Unreleased Structures]]
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5h55|5h55]], [[5h54|5h54]], [[5h5c|5h5c]]</td></tr>
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<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=5h5a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h5a OCA], [http://pdbe.org/5h5a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h5a RCSB], [http://www.ebi.ac.uk/pdbsum/5h5a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h5a ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/MDM12_KLULA MDM12_KLULA]] Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. MDM12 is required for the interaction of the ER-resident membrane protein MMM1 and the outer mitochondrial membrane-resident beta-barrel protein MDM10. The MDM12-MMM1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all mitochondrial outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The MDM10-MDM12-MMM1 subcomplex further acts in the TOM40-specific pathway after the action of the MDM12-MMM1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids.
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__TOC__
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</StructureSection>
[[Category: Endo, T]]
[[Category: Endo, T]]
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[[Category: Kawano, S]]
[[Category: Quinbara, S]]
[[Category: Quinbara, S]]
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[[Category: Kawano, S]]
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[[Category: Lipid binding protein]]

Revision as of 07:46, 8 November 2017

Mdm12 from K. lactis (1-239), Lys residues are uniformly dimethyl modified

5h5a, resolution 2.26Å

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