Thiolase
From Proteopedia
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3D Structures of Thiolase
Updated on 06-October-2017 {{#tree:id=OrganizedByTopic|openlevels=0|
- 3-ketoacyl-CoA thiolase
- 2wu9, 2c7y, 2c7z – KCT peroxisomal residues 36-462 – Arabidopsis thaliana
- 2wua - KCT peroxisomal residues 17-449 (mutant) – sunflower
- 2iik – hKCT peroxisomal – human
- 4c2k – hKCT mitochondrial
- 4c2j – hKCT mitochondrial + CoA
- 3goa – KCT – Salmonella typhimurium
- 5lp7 – KCT – Bacillus subtilis
- 1afw, 1pxt – yKCT peroxisomal – yeast
- 5cbq – MsKCT – Mycobacterium smegmatis
- 4w61 – ReKCT – Ralstonia eutropha
- 4ubw – MtKCT – Mycobacterium tuberculosis
- 2wu9, 2c7y, 2c7z – KCT peroxisomal residues 36-462 – Arabidopsis thaliana
- 3-ketoacyl-CoA thiolase complex
- 3w15 - yKCT peroxisomal residues 27-396 + peroxiomal membrane protein PEX21 + peroxisomal targeting signal receptor
- 2d3t – PfKCT + fatty oxidation complex β subunit – Pseudomonas fragi
- 1wdk, 1wdl, 1wdm - PfKCT + fatty oxidation complex α subunit
- 5bz4 – MsKCT + CoA
- 4ubt – MtKCT (mutant) + CoA + steroid
- 4ubu – MtKCT (mutant) + CoA
- 4ubv – MtKCT + CoA + acetyl CoA
- 3w15 - yKCT peroxisomal residues 27-396 + peroxiomal membrane protein PEX21 + peroxisomal targeting signal receptor
- Acetoacetyl-CoA thiolase
- 1m4s, 1m4t, 1dlu, 1qfl - ZrACT – Zoogloea ramigera
- 2wku, 2wl6, 1m1t, 1m3k - ZrACT (mutant)
- 2ib7, 2ib8, 2ib9, 2ibu, 2ibw, 2iby, 2f2s – hACT mitochondrial
- 1wl5 - hACT cytosolic
- 4dd5, 4e1l – ACT – Clostridium difficile
- 4xl2, 4xl3, 4n44, 4n45 – CaACT – Clostridium acetobutylicum
- 4wyr – CaACT (mutant)
- 5f0v, [[ 5f38, 4wys – ACT – Escherichia coli
- 4o9a, 4o99, 4o9c, 4nzs – ReACT
- 1m4s, 1m4t, 1dlu, 1qfl - ZrACT – Zoogloea ramigera
- Acetoacetyl-CoA thiolase complex
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References
- ↑ Sundaramoorthy R, Micossi E, Alphey MS, Germain V, Bryce JH, Smith SM, Leonard GA, Hunter WN. The crystal structure of a plant 3-ketoacyl-CoA thiolase reveals the potential for redox control of peroxisomal fatty acid beta-oxidation. J Mol Biol. 2006 Jun 2;359(2):347-57. Epub 2006 Mar 29. PMID:16630629 doi:http://dx.doi.org/10.1016/j.jmb.2006.03.032
- ↑ Soto G, Stritzler M, Lisi C, Alleva K, Pagano ME, Ardila F, Mozzicafreddo M, Cuccioloni M, Angeletti M, Ayub ND. Acetoacetyl-CoA thiolase regulates the mevalonate pathway during abiotic stress adaptation. J Exp Bot. 2011 Nov;62(15):5699-711. doi: 10.1093/jxb/err287. Epub 2011 Sep 9. PMID:21908473 doi:http://dx.doi.org/10.1093/jxb/err287
- ↑ Kiema TR, Harijan RK, Strozyk M, Fukao T, Alexson SE, Wierenga RK. The crystal structure of human mitochondrial 3-ketoacyl-CoA thiolase (T1): insight into the reaction mechanism of its thiolase and thioesterase activities. Acta Crystallogr D Biol Crystallogr. 2014 Dec 1;70(Pt 12):3212-25. doi:, 10.1107/S1399004714023827. Epub 2014 Nov 22. PMID:25478839 doi:http://dx.doi.org/10.1107/S1399004714023827