Malate synthase

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== Structural highlights ==
== Structural highlights ==
MS active site pocket is situated between the TIM barrle and the C-terminal. The ternary complex contains malate, acetyl-CoA and Mg+2 ion<ref>PMID:16877713</ref>.
MS active site pocket is situated between the TIM barrle and the C-terminal. The ternary complex contains malate, acetyl-CoA and Mg+2 ion<ref>PMID:16877713</ref>.
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<scene name='57/573146/Cv/3'>Malate/Mg+2 ion binding site</scene>. Water molecules shown as red spheres.
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<scene name='57/573146/Cv/6'>Acetyl-CoA binding site</scene>.
</StructureSection>
</StructureSection>

Revision as of 09:29, 19 April 2016

Structure of malate synthase G complex with CoA, malate, Hepes and Mg+2 ion (green) (PDB entry 2gq3)

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3d structures of malate synthase

Updated on 19-April-2016

References

  1. Anstrom DM, Kallio K, Remington SJ. Structure of the Escherichia coli malate synthase G:pyruvate:acetyl-coenzyme A abortive ternary complex at 1.95 A resolution. Protein Sci. 2003 Sep;12(9):1822-32. PMID:12930982
  2. Anstrom DM, Remington SJ. The product complex of M. tuberculosis malate synthase revisited. Protein Sci. 2006 Aug;15(8):2002-7. PMID:16877713 doi:15/8/2002

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