2GTV
NMR structure of monomeric chorismate mutase from Methanococcus jannaschii
Summary for 2GTV
| Entry DOI | 10.2210/pdb2gtv/pdb |
| NMR Information | BMRB: 7093 |
| Descriptor | chorismate mutase, 8-HYDROXY-2-OXA-BICYCLO[3.3.1]NON-6-ENE-3,5-DICARBOXYLIC ACID (2 entities in total) |
| Functional Keywords | four-helix bundle, isomerase |
| Biological source | Methanocaldococcus jannaschii |
| Total number of polymer chains | 1 |
| Total formula weight | 12740.72 |
| Authors | Vogeli, B.R. (deposition date: 2006-04-28, release date: 2006-10-31, Last modification date: 2024-05-29) |
| Primary citation | Pervushin, K.,Vamvaca, K.,Vogeli, B.,Hilvert, D. Structure and dynamics of a molten globular enzyme. Nat.Struct.Mol.Biol., 14:1202-1206, 2007 Cited by PubMed Abstract: 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. PubMed: 17994104DOI: 10.1038/nsmb1325 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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