Crystallization and preliminary structural analyses of glutamate dehydrogenase from Peptoniphilus asaccharolyticus

Glutamate dehydrogenase (EC 1.4.1.2–4) from Peptoniphilus asaccharolyticus has been expressed as a selenomethionine‐derivatized recombinant protein and diffraction‐quality crystals have been grown that are suitable for structure determination. Preliminary structural analyses indicate that the protei...

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Veröffentlicht in:Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2010-05, Vol.66 (5), p.523-526
Hauptverfasser: Oliveira, Tania F., Carrigan, John B., Hamza, Muaawia A., Sharkey, Michael A., Engel, Paul C., Khan, Amir R.
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Sprache:eng
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Zusammenfassung:Glutamate dehydrogenase (EC 1.4.1.2–4) from Peptoniphilus asaccharolyticus has been expressed as a selenomethionine‐derivatized recombinant protein and diffraction‐quality crystals have been grown that are suitable for structure determination. Preliminary structural analyses indicate that the protein assembles as a homohexameric enzyme complex in solution, similar to other bacterial and mammalian enzymes to which its sequence identity varies between 25 and 40%. The structure will provide insight into its preference for the cofactor NADH (over NADPH) by comparisons with the known structures of mammalian and bacterial enzymes.
ISSN:1744-3091
1744-3091
2053-230X
DOI:10.1107/S1744309110010006