4ped: Difference between revisions

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'''Unreleased structure'''
==Mitochondrial ADCK3 employs an atypical protein kinase-like fold to enable coenzyme Q biosynthes==
 
<StructureSection load='4ped' size='340' side='right' caption='[[4ped]], [[Resolution|resolution]] 1.64&Aring;' scene=''>
The entry 4ped is ON HOLD
== Structural highlights ==
 
<table><tr><td colspan='2'>[[4ped]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PED OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PED FirstGlance]. <br>
Authors: Bingman, C.A., Smith, R., Joshi, S., Stefely, J.A., Reidenbach, A.G., Ulbrich, A., Oruganty, O., Floyd, B.J., Jochem, A., Saunders, J.M., Johnson, I.E., Wrobel, R.L., Barber, G.E., Lee, D., Li, S., Kannan, N., Coon, J.J., Pagliarini, D.J., Mitochondrial Protein Partnership (MPP)
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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>
Description: Structure of mitochondrial ADCK3 defines an ancient protein kinase-like fold
<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=4ped FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ped OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ped RCSB], [http://www.ebi.ac.uk/pdbsum/4ped PDBsum]</span></td></tr>
</table>
== Disease ==
[[http://www.uniprot.org/uniprot/ADCK3_HUMAN ADCK3_HUMAN]] Autosomal recessive ataxia due to ubiquinone deficiency. The disease is caused by mutations affecting the gene represented in this entry.  
== Function ==
[[http://www.uniprot.org/uniprot/ADCK3_HUMAN ADCK3_HUMAN]] Putative protein kinase involved in the biosynthesis of coenzyme Q since it is able to rescue partially coenzyme Q6 biosynthesis of yeast COQ8 mutants. May be a chaperone-like protein essential for the proper conformation and functioning of protein complexes in the respiratory chain.<ref>PMID:21296186</ref> 
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Barber, G E]]
[[Category: Bingman, C A]]
[[Category: Coon, J J]]
[[Category: Floyd, B J]]
[[Category: Jochem, A]]
[[Category: Johnson, I E]]
[[Category: Joshi, S]]
[[Category: Kannan, N]]
[[Category: Lee, D]]
[[Category: Li, S]]
[[Category: MPP, Mitochondrial Protein Partnership]]
[[Category: Oruganty, O]]
[[Category: Pagliarini, D J]]
[[Category: Reidenbach, A G]]
[[Category: Saunders, J M]]
[[Category: Smith, R]]
[[Category: Stefely, J A]]
[[Category: Ulbrich, A]]
[[Category: Wrobel, R L]]
[[Category: Coenzyme q biosynthesis]]
[[Category: Membrane associated]]
[[Category: Mitochondrial]]
[[Category: Mitochondrial protein partnership]]
[[Category: Mpp]]
[[Category: Protein kinase-like]]
[[Category: Psi-biology]]
[[Category: Structural genomic]]
[[Category: Transferase]]
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