PDBsum entry: 2gtv

Isomerase

PDB id: 2gtv

Contents

Protein chain

104 a.a. *

Ligands

TSA

* Residue conservation analysis

PDB id:

2gtv

Name:

Isomerase

Title:

Nmr structure of monomeric chorismate mutase from methanococcus jannaschii

Structure:

Chorismate mutase. Chain: x. Synonym: cm. Hypothetical protein mj0246. Engineered: yes

Source:

Methanocaldococcus jannaschii. Organism_taxid: 2190. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

10 models

Authors:

B.R.Vogeli

Key ref:

K.Pervushin et al. (2007). Structure and dynamics of a molten globular enzyme. Nat Struct Biol, 14, 1202-1206. PubMed id: 17994104 DOI: 10.1038/nsmb1325

Date:

28-Apr-06 Release date: 31-Oct-06

Protein chain

Q57696  (Y246_METJA) -  Uncharacterized protein MJ0246

Seq: 99 a.a.

Struc: 104 a.a.*

* PDB and UniProt seqs differ at 12 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 

• Biological process: chorismate metabolic process (1 term)

DOI no: 10.1038/nsmb1325

Nat Struct Biol 14:1202-1206 (2007)

PubMed id: 17994104

Structure and dynamics of a molten globular enzyme.

K.Pervushin, K.Vamvaca, B.Vögeli, D.Hilvert.

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.

Selected figure(s)

Figure 1.
(a) Left, conversion of chorismate to prephenate catalyzed by the enzyme. Right, a conformationally constrained oxabicyclic dicarboxylic acid TSA^13. (b) Model of the 96-residue monomer based on the X-ray structure of the EcCM complex with the TSA. (c) The ten lowest-energy conformers of the mMjCM–TSA NMR structure. The engineered loop, residues 23a–h, is shown in red. The TSA, which binds at the active site, is shown in ball-and-stick representation. (d) Structure of the mMjCM dimer that forms at high protein concentration.

Figure 2.
The polar residues (cyan) that contact the TSA (yellow) are superimposed on their counterparts from the EcCM crystal structure (pink). Amino acid numbering is based on the EcCM sequence^13.

The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Biol (2007, 14, 1202-1206) copyright 2007.

Figures were selected by an automated process.