2gtv
From Proteopedia
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'''NMR structure of monomeric chorismate mutase from Methanococcus jannaschii''' | '''NMR structure of monomeric chorismate mutase from Methanococcus jannaschii''' | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Vogeli, B R.]] | [[Category: Vogeli, B R.]] | ||
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Revision as of 02:32, 4 May 2008
NMR structure of monomeric chorismate mutase from Methanococcus jannaschii
Overview
Although protein dynamics has been recognized as a potentially important contributor to enzyme catalysis, structural disorder is generally considered to reduce catalytic efficiency. This widely held assumption has recently been challenged by the finding that an engineered chorismate mutase combines high catalytic activity with the properties of a molten globule, a loosely packed and highly dynamic conformational ensemble. Taking advantage of the ordering observed upon ligand binding, we have now used NMR spectroscopy to characterize this enzyme in complex with a transition-state analog. The complex adopts a helix-bundle structure, as designed, but retains unprecedented flexibility on the millisecond timescale across its entire length. Moreover, pre-steady-state kinetics data show that binding occurs by an induced-fit mechanism on the same timescale as the enzymatic reaction, linking global conformational plasticity with efficient catalysis.
About this Structure
2GTV is a Single protein structure of sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA.
Reference
Structure and dynamics of a molten globular enzyme., Pervushin K, Vamvaca K, Vogeli B, Hilvert D, Nat Struct Mol Biol. 2007 Dec;14(12):1202-6. Epub 2007 Nov 11. PMID:17994104 Page seeded by OCA on Sun May 4 05:31:58 2008
