3NRI

Crystal structure of the C(30) carotenoid dehydrosqualene synthase from S. aureus complexed with dehydrosqualene (DHS)


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.85 Å
  • R-Value Free: 0.307 
  • R-Value Work: 0.206 
  • R-Value Observed: 0.211 

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This is version 1.2 of the entry. See complete history


Literature

Mechanism of action and inhibition of dehydrosqualene synthase.

Lin, F.Y.Liu, C.I.Liu, Y.L.Zhang, Y.Wang, K.Jeng, W.Y.Ko, T.P.Cao, R.Wang, A.H.Oldfield, E.

(2010) Proc Natl Acad Sci U S A 107: 21337-21342

  • DOI: https://doi.org/10.1073/pnas.1010907107
  • Primary Citation of Related Structures:  
    3ACW, 3ACX, 3ACY, 3ADZ, 3AE0, 3LGZ, 3NPR, 3NRI

  • PubMed Abstract: 

    "Head-to-head" terpene synthases catalyze the first committed steps in sterol and carotenoid biosynthesis: the condensation of two isoprenoid diphosphates to form cyclopropylcarbinyl diphosphates, followed by ring opening. Here, we report the structures of Staphylococcus aureus dehydrosqualene synthase (CrtM) complexed with its reaction intermediate, presqualene diphosphate (PSPP), the dehydrosqualene (DHS) product, as well as a series of inhibitors. The results indicate that, on initial diphosphate loss, the primary carbocation so formed bends down into the interior of the protein to react with C2,3 double bond in the prenyl acceptor to form PSPP, with the lower two-thirds of both PSPP chains occupying essentially the same positions as found in the two farnesyl chains in the substrates. The second-half reaction is then initiated by the PSPP diphosphate returning back to the Mg(2+) cluster for ionization, with the resultant DHS so formed being trapped in a surface pocket. This mechanism is supported by the observation that cationic inhibitors (of interest as antiinfectives) bind with their positive charge located in the same region as the cyclopropyl carbinyl group; that S-thiolo-diphosphates only inhibit when in the allylic site; activity results on 11 mutants show that both DXXXD conserved domains are essential for PSPP ionization; and the observation that head-to-tail isoprenoid synthases as well as terpene cyclases have ionization and alkene-donor sites which spatially overlap those found in CrtM.


  • Organizational Affiliation

    Center for Biophysics and Computational Biology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Dehydrosqualene synthase293Staphylococcus aureus subsp. aureus A017934/97Mutation(s): 0 
Gene Names: crtmSHAG_00345
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
DH7
Query on DH7

Download Ideal Coordinates CCD File 
B [auth A](6E,10R,13S,18E)-2,6,10,15,19,23-hexamethyltetracosa-2,6,10,11,13,14,18,22-octaene
C30 H46
PALVLARMLPXARO-HCTXVGCHSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.85 Å
  • R-Value Free: 0.307 
  • R-Value Work: 0.206 
  • R-Value Observed: 0.211 
  • Space Group: P 32 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 80.585α = 90
b = 80.585β = 90
c = 90.363γ = 120
Software Package:
Software NamePurpose
HKL-2000data collection
PHASERphasing
REFMACrefinement
HKL-2000data reduction
HKL-2000data scaling

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-12-22
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2023-12-27
    Changes: Data collection, Database references, Derived calculations