4CSM

YEAST CHORISMATE MUTASE + TYR + ENDOOXABICYCLIC INHIBITOR


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • R-Value Free: 0.270 
  • R-Value Work: 0.213 
  • R-Value Observed: 0.213 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Mechanisms of catalysis and allosteric regulation of yeast chorismate mutase from crystal structures.

Strater, N.Schnappauf, G.Braus, G.Lipscomb, W.N.

(1997) Structure 5: 1437-1452

  • DOI: https://doi.org/10.1016/s0969-2126(97)00294-3
  • Primary Citation of Related Structures:  
    3CSM, 4CSM, 5CSM

  • PubMed Abstract: 

    Chorismate mutase (CM) catalyzes the Claisen rearrangement of chorismate to prephenate, notably the only known enzymatically catalyzed pericyclic reaction in primary metabolism. Structures of the enzyme in complex with an endo-oxabicyclic transition state analogue inhibitor, previously determined for Bacillus subtilis and Escherichia coli CM, provide structural insight into the enzyme mechanism. In contrast to these bacterial CMs, yeast CM is allosterically regulated in two ways: activation by tryptophan and inhibition by tyrosine. Yeast CM exists in two allosteric states, R (active) and t (inactive).


  • Organizational Affiliation

    Department of Chemistry and Chemical Biology, Harvard University, 12 Oxford Street, Cambridge, MA 02138, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
CHORISMATE MUTASE
A, B
256Saccharomyces cerevisiaeMutation(s): 0 
EC: 5.4.99.5
UniProt
Find proteins for P32178 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore P32178 
Go to UniProtKB:  P32178
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP32178
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
TSA
Query on TSA

Download Ideal Coordinates CCD File 
D [auth A],
F [auth B]
8-HYDROXY-2-OXA-BICYCLO[3.3.1]NON-6-ENE-3,5-DICARBOXYLIC ACID
C10 H12 O6
KRZHNRULRHECRF-JQCUSGDOSA-N
TYR
Query on TYR

Download Ideal Coordinates CCD File 
C [auth A],
E [auth B]
TYROSINE
C9 H11 N O3
OUYCCCASQSFEME-QMMMGPOBSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • R-Value Free: 0.270 
  • R-Value Work: 0.213 
  • R-Value Observed: 0.213 
  • Space Group: H 3 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 205.5α = 90
b = 205.5β = 90
c = 131.2γ = 120
Software Package:
Software NamePurpose
XDSdata scaling
XDSdata reduction
AMoREphasing
X-PLORrefinement

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1998-01-14
    Type: Initial release
  • Version 1.1: 2008-03-25
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Derived calculations, Version format compliance
  • Version 1.3: 2023-08-09
    Changes: Database references, Derived calculations, Refinement description