SCP2-thiolase
From Proteopedia
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The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>. | The A-monomer is the single monomer, and the B-monomer is forming a dimer with its two-fold crystallographically related <scene name='80/809821/6hsp-dimer/5'>symmetry copy</scene>. | ||
| - | The active site is at the <scene name='80/809821/6hsp-dimer_active_site/2'>dimer interface</scene> | + | Each subunit can be divied in an N-termial domain, a loop domain and a C-terminal domain. |
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| + | The active site is at the <scene name='80/809821/6hsp-dimer_active_site/2'>dimer interface</scene>. | ||
The active site is shaped by the residues of <scene name='80/809821/6hsp-dimer-catalytic-residues/2'>four loops</scene> | The active site is shaped by the residues of <scene name='80/809821/6hsp-dimer-catalytic-residues/2'>four loops</scene> | ||
Revision as of 18:47, 10 April 2019
Structure of the zebrafish SCP2-thiolase [1]
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References
- ↑ Kiema TR, Thapa CJ, Laitaoja M, Schmitz W, Maksimainen MM, Fukao T, Rouvinen J, Janis J, Wierenga RK. The peroxisomal zebrafish SCP2-thiolase (type-1) is a weak transient dimer as revealed by crystal structures and native mass spectrometry. Biochem J. 2018 Dec 20. pii: BCJ20180788. doi: 10.1042/BCJ20180788. PMID:30573650 doi:http://dx.doi.org/10.1042/BCJ20180788
- ↑ Anbazhagan P, Harijan RK, Kiema TR, Janardan N, Murthy MR, Michels PA, Juffer AH, Wierenga RK. Phylogenetic relationships and classification of thiolases and thiolase-like proteins of Mycobacterium tuberculosis and Mycobacterium smegmatis. Tuberculosis (Edinb). 2014 Jul;94(4):405-12. doi: 10.1016/j.tube.2014.03.003., Epub 2014 Apr 4. PMID:24825023 doi:http://dx.doi.org/10.1016/j.tube.2014.03.003
- ↑ Antonenkov VD, Van Veldhoven PP, Waelkens E, Mannaerts GP. Substrate specificities of 3-oxoacyl-CoA thiolase A and sterol carrier protein 2/3-oxoacyl-CoA thiolase purified from normal rat liver peroxisomes. Sterol carrier protein 2/3-oxoacyl-CoA thiolase is involved in the metabolism of 2-methyl-branched fatty acids and bile acid intermediates. J Biol Chem. 1997 Oct 10;272(41):26023-31. PMID:9325339
- ↑ Ferdinandusse S, Kostopoulos P, Denis S, Rusch H, Overmars H, Dillmann U, Reith W, Haas D, Wanders RJ, Duran M, Marziniak M. Mutations in the gene encoding peroxisomal sterol carrier protein X (SCPx) cause leukencephalopathy with dystonia and motor neuropathy. Am J Hum Genet. 2006 Jun;78(6):1046-52. Epub 2006 Mar 29. PMID:16685654 doi:10.1086/503921
