2-oxoisovalerate dehydrogenase

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== Structural highlights ==
== Structural highlights ==
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<scene name='80/800706/Cv/3'>Human 2-oxoisovalerate dehydrogenase α and β subunit with phosphorylated Ser residue complex with thiamine diphosphate, glycerol, K+ ion, Cl- ion, and Mn+2 ion</scene>. The structure of the phosphorylated human OIVD shows the <scene name='80/800706/Cv/8'>cofactor ThDP interacting with residues from both α and β subunits</scene> (water molecules shown as red spheres) and the phosphorylated Ser292 residue. Phosphorylation of Ser292 of the α subunit interferes with ThDP binding<ref>PMID:15576032</ref>.
+
<scene name='80/800706/Cv/3'>Human 2-oxoisovalerate dehydrogenase α and β subunit with phosphorylated Ser residue complex with thiamine diphosphate, glycerol, K+ ion, Cl- ion, and Mn+2 ion</scene>. The structure of the phosphorylated human OIVD shows the <scene name='80/800706/Cv/8'>cofactor ThDP interacting with residues from both α and β subunits</scene> (water molecules shown as red spheres). Phosphorylation of Ser292 of the α subunit interferes with ThDP binding<ref>PMID:15576032</ref>.
*<scene name='80/800706/Cv/9'>Mn coordination site</scene>.
*<scene name='80/800706/Cv/9'>Mn coordination site</scene>.
*<scene name='80/800706/Cv/10'>Cl coordination site</scene>.
*<scene name='80/800706/Cv/10'>Cl coordination site</scene>.

Revision as of 12:01, 16 December 2018

Human 2-oxoisovalerate dehydrogenase α (deepskyblue and cyan) and β (coral and orangered) subunit with phosphorylated Ser residue complex with thiamine diphosphate, glycerol, K+ ion (purple), Cl- ion (green) and Mn+2 ion (PDB code 1x80)

Drag the structure with the mouse to rotate

3D structures of 2-oxoisovalerate dehydrogenase

Updated on 16-December-2018

2bp7 - OIVD α+β subunits - Pseudomonas putida
1v1r - hOIVD α+β subunits - human
1u5b, 1x80, 1ols - hOIVD α+β subunits + ThDP
1x7x, 1x7w, 1x7y, 1x7z, 2j9f, 1olu, 2bfb, 2bfd, 2bfe, 1v11 - hOIVD α (mutant)+ β subunits + ThDP derivative
1olx - hOIVD α+β (mutant) subunits + ThDP
1wci - hOIVD α+β subunits + thiamine derivative
2bfe - hOIVD α+β subunits + pyrimidine derivative
2bfc - hOIVD α (mutant)+ β subunits + pyrimidine derivative
1v16 - hOIVD α+β subunits + ThDP + benzamidine
1v1m - hOIVD α (mutant)+ β subunits + ThDP + benzamidine
2bew, 2beu, 2bev - hOIVD α+β subunits + ThDP derivative + peptide

References

  1. ↑ Aevarsson A, Seger K, Turley S, Sokatch JR, Hol WG. Crystal structure of 2-oxoisovalerate and dehydrogenase and the architecture of 2-oxo acid dehydrogenase multienzyme complexes. Nat Struct Biol. 1999 Aug;6(8):785-92. PMID:10426958 doi:10.1038/11563
  2. ↑ Wang YP, Qi ML, Li TT, Zhao YJ. Two novel mutations in the BCKDHB gene (R170H, Q346R) cause the classic form of maple syrup urine disease (MSUD). Gene. 2012 Apr 25;498(1):112-5. doi: 10.1016/j.gene.2012.01.082. Epub 2012 Feb 3. PMID:22326532 doi:10.1016/j.gene.2012.01.082
  3. ↑ Wynn RM, Kato M, Machius M, Chuang JL, Li J, Tomchick DR, Chuang DT. Molecular mechanism for regulation of the human mitochondrial branched-chain alpha-ketoacid dehydrogenase complex by phosphorylation. Structure. 2004 Dec;12(12):2185-96. PMID:15576032 doi:10.1016/j.str.2004.09.013

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