2-isopropylmalate synthase
From Proteopedia
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| - | <StructureSection load=' | + | <StructureSection load='3fig' size='340' side='right' caption='2-isopropylmalate synthase complex with leucine, glycerol and Zn+2 ion (grey) (PDB code [[3fig]])' scene=''> |
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== Structural highlights == | == Structural highlights == | ||
| - | + | LeuA structure is composed of 2 major domains - the catalytic N-terminal and the regulatory C-terminal. The 2 domains are separated by subdomains I and II and a short flexible hinge region between the 2 subdomains. The catalytic domain binds the substrate and the Zn+2 ion<ref>PMID:15159544</ref>. | |
</StructureSection> | </StructureSection> | ||
==3D structures of 2-isopropylmalate synthase== | ==3D structures of 2-isopropylmalate synthase== | ||
Revision as of 11:12, 19 December 2016
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3D structures of 2-isopropylmalate synthase
Updated on 19-December-2016
References
- ↑ de Carvalho LP, Blanchard JS. Kinetic and chemical mechanism of alpha-isopropylmalate synthase from Mycobacterium tuberculosis. Biochemistry. 2006 Jul 25;45(29):8988-99. PMID:16846242 doi:http://dx.doi.org/10.1021/bi0606602
- ↑ Koon N, Squire CJ, Baker EN. Crystal structure of LeuA from Mycobacterium tuberculosis, a key enzyme in leucine biosynthesis. Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8295-300. Epub 2004 May 24. PMID:15159544 doi:10.1073/pnas.0400820101
