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>. | ||
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| + | The active site is at the <scene name='80/809821/6hsp-dimer_active_site/1'>dimer interface</scene> | ||
== Function == | == Function == | ||
Revision as of 08:00, 8 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
- ↑ Venkatesan R, Sah-Teli SK, Awoniyi LO, Jiang G, Prus P, Kastaniotis AJ, Hiltunen JK, Wierenga RK, Chen Z. Insights into mitochondrial fatty acid synthesis from the structure of heterotetrameric 3-ketoacyl-ACP reductase/3R-hydroxyacyl-CoA dehydrogenase. Nat Commun. 2014 Sep 9;5:4805. doi: 10.1038/ncomms5805. PMID:25203508 doi:http://dx.doi.org/10.1038/ncomms5805
