NDLI: Crystallization and preliminary X-ray diffraction analysis of various enzyme-substrate complexes of isopropylmalate dehydrogenase from Thermus thermophilus.

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Crystallization and preliminary X-ray diffraction analysis of various enzyme-substrate complexes of isopropylmalate dehydrogenase from Thermus thermophilus.

Content Provider	Europe PMC
Author	Merli, Angelo Manikandan, Karuppasamy Gráczer, Éva Schuldt, Linda Singh, Rajesh Kumar Závodszky, Péter Vas, Mária Weiss, Manfred S.
Copyright Year	2010
Description	The enzyme 3-isopropylmalate dehydrogenase (IPMDH) from T. thermophilus, which catalyses the penultimate reaction step of the leucine-biosynthesis pathway, has been crystallized in various states along its reaction coordinate. The Thermus thermophilus 3-isopropylmalate dehydrogenase (Tt-IPMDH) enzyme catalyses the penultimate step of the leucine-biosynthesis pathway. It converts (2R,3S)-3-isopropylmalate to (2S)-2-isopropyl-3-oxosuccinate in the presence of divalent Mg2+ or Mn2+ and with the help of NAD+. In order to elucidate the detailed structural and functional mode of the enzymatic reaction, crystals of Tt-IPMDH were grown in the presence of various combinations of substrate and/or cofactors. Here, the crystallization, data collection and preliminary crystallographic analyses of six such complexes are reported.
Related Links	https://europepmc.org/backend/ptpmcrender.fcgi?accid=PMC2882784&blobtype=pdf
Volume Number	66
PubMed Central reference number	PMC2882784
Issue Number	Pt 6
Issue Number	pt 6
PubMed reference number	20516614
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications [Acta Crystallogr Sect F Struct Biol Cryst Commun]
e-ISSN	17443091
DOI	10.1107/s174430911001626x
Language	English
Publisher	International Union of Crystallography
Publisher Date	2010-05-29
Access Restriction	Open
Rights License	© International Union of Crystallography 2010
Subject Keyword	isopropylmalate dehydrogenase Thermus thermophilus leucine-biosynthesis pathway
Content Type	Text
Resource Type	Article
Subject	Biochemistry Condensed Matter Physics Genetics Biophysics Structural Biology

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