Thiolase
From Proteopedia
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</StructureSection> | </StructureSection> | ||
| - | == 3D Structures of Thiolase == | ||
| - | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
| - | {{#tree:id=OrganizedByTopic|openlevels=0| | ||
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| - | *3-ketoacyl-CoA thiolase | ||
| - | |||
| - | **[[2iik]] – hKCT peroxisomal – human<br /> | ||
| - | **[[4c2k]] – hKCT mitochondrial <br /> | ||
| - | **[[4c2j]] – hKCT mitochondrial + CoA<br /> | ||
| - | **[[2wu9]], [[2c7y]], [[2c7z]] – KCT peroxisomal residues 36-462 – ''Arabidopsis thaliana''<br /> | ||
| - | **[[2wua]] - KCT peroxisomal residues 17-449 (mutant) – sunflower<br /> | ||
| - | **[[1afw]], [[1pxt]] – yKCT peroxisomal – yeast<br /> | ||
| - | **[[3goa]] – KCT – ''Salmonella typhimurium''<br /> | ||
| - | **[[5lp7]] – KCT – ''Bacillus subtilis'' <br /> | ||
| - | **[[5cbq]] – MsKCT – ''Mycobacterium smegmatis'' <br /> | ||
| - | **[[4w61]] – ReKCT – ''Ralstonia eutropha''<br /> | ||
| - | **[[4ubw]], [[5onc]] – MtKCT – ''Mycobacterium tuberculosis'' <br /> | ||
| - | |||
| - | *3-ketoacyl-CoA thiolase complex | ||
| - | |||
| - | **[[3w15]] - yKCT peroxisomal residues 27-396 + peroxiomal membrane protein PEX21 + peroxisomal targeting signal receptor<br /> | ||
| - | **[[2d3t]] – PfKCT + fatty oxidation complex β subunit – ''Pseudomonas fragi''<br /> | ||
| - | **[[1wdk]], [[1wdl]], [[1wdm]] - PfKCT + fatty oxidation complex α subunit<br /> | ||
| - | **[[5bz4]] – MsKCT + CoA <br /> | ||
| - | **[[4ubt]] – MtKCT (mutant) + CoA + steroid <br /> | ||
| - | **[[4ubu]] – MtKCT (mutant) + CoA <br /> | ||
| - | **[[4ubv]] – MtKCT + CoA + acetyl CoA <br /> | ||
| - | |||
| - | *Acetoacetyl-CoA thiolase or acetyl-CoA acetyltransferase | ||
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| - | **[[2ib7]], [[2ib8]], [[2ib9]], [[2ibu]], [[2ibw]], [[2iby]], [[2f2s]] – hACT mitochondrial<br /> | ||
| - | **[[1wl5]] - hACT cytosolic<br /> | ||
| - | **[[5xyj]], [[5xz5]] – yACT <br /> | ||
| - | **[[1m4s]], [[1m4t]], [[1dlu]], [[1qfl]] - ZrACT – ''Zoogloea ramigera''<br /> | ||
| - | **[[2wku]], [[2wl6]], [[1m1t]], [[1m3k]] - ZrACT (mutant) <br /> | ||
| - | **[[4dd5]], [[4e1l]] – ACT – ''Clostridium difficile''<br /> | ||
| - | **[[4xl2]], [[4xl3]], [[4n44]], [[4n45]] – CaACT – ''Clostridium acetobutylicum''<br /> | ||
| - | **[[4wyr]] – CaACT (mutant) <br /> | ||
| - | **[[5f0v]], [[5f38]], [[4wys]] – ACT – ''Escherichia coli'' <br /> | ||
| - | **[[4o9a]], [[4o99]], [[4o9c]], [[4nzs]] – ReACT <br /> | ||
| - | |||
| - | *Acetoacetyl-CoA thiolase complex | ||
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| - | **[[1wl4]] – hACT cytosolic + CoA <br /> | ||
| - | **[[1dm3]], [[1dlv]] – ZrACT + CoA<br /> | ||
| - | **[[2wkt]], [[2wkv]], [[2wl4]], [[2wl5]], [[2vtz]], [[1m3z]] – ZrACT (mutant) + CoA<br /> | ||
| - | **[[1m1o]] - ZrACT (mutant) + acetoacetyl-CoA<br /> | ||
| - | **[[2vu0]], [[1nl7]] - ZrACT + CoA<br /> | ||
| - | **[[2vu1]], [[2vu2]], [[1ou6]] - ZrACT + pantheteine-11-pivalate<br /> | ||
| - | **[[4xl4]] – CaACT + CoA <br /> | ||
| - | **[[6et9]] – MtACT + PFAM DUF35 + hydroxymethylglutaryl-CoA synthase - ''Methanothermococcus thermolithotrophicus''<br /> | ||
| - | **[[6esq]] – MtACT + CoA + PFAM DUF35 + hydroxymethylglutaryl-CoA synthase <br /> | ||
| - | **[[6are]] – ACT + CoA + acetate - ''Aspergillus fumigatus'' <br /> | ||
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| - | *SCP2-thiolase | ||
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| - | **]]6hrv]] – zfSCP2 - zebrafish <br /> | ||
| - | **]]6hsj]] – zfSCP2 + CoA<br /> | ||
| - | **]]6hsp]] – zfSCP2 + CoA + octanoyl-CoA<br /> | ||
| - | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 11:02, 20 February 2020
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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
