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2-isopropylmalate synthase

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== Structural highlights ==
== Structural highlights ==
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<scene name='74/748866/Cv/2'>Domain organization of LeuA</scene>. LeuA structure is composed of 2 major domains - the catalytic N-terminal which shows a TIM barrel conformation 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 <scene name='74/748866/Cv/3'>Zn+2 ion</scene><ref>PMID:15159544</ref>.
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<scene name='74/748866/Cv/2'>Domain organization of LeuA</scene>. LeuA structure is composed of 2 major domains - the catalytic N-terminal which shows a TIM barrel conformation 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 <scene name='74/748866/Cv/3'>Zn+2 ion</scene><ref>PMID:15159544</ref>. <scene name='74/748866/Cv/4'>Leucine binding site</scene>.
</StructureSection>
</StructureSection>
==3D structures of 2-isopropylmalate synthase==
==3D structures of 2-isopropylmalate synthase==

Revision as of 08:39, 3 August 2017

2-isopropylmalate synthase complex with leucine, glycerol and Zn+2 ion (grey) (PDB code 3fig)

Drag the structure with the mouse to rotate

3D structures of 2-isopropylmalate synthase

Updated on 03-August-2017

References

  1. ↑ 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
  2. ↑ 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

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Michal Harel, Alexander Berchansky, Joel L. Sussman

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