RCSB PDB - 6A99: Crystal structure of a Stig cyclases Fisc from Fischerella sp. TAU in complex with (3Z)-3-(1-methyl-2-pyrrolidinylidene)-3H-indole

 6A99

Crystal structure of a Stig cyclases Fisc from Fischerella sp. TAU in complex with (3Z)-3-(1-methyl-2-pyrrolidinylidene)-3H-indole


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.29 Å
  • R-Value Free: 0.241 
  • R-Value Work: 0.187 
  • R-Value Observed: 0.190 

Starting Model: experimental
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Ligand Structure Quality Assessment 

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Literature

The Crystal Structure of a Class of Cyclases that Catalyze the Cope Rearrangement

Chen, C.C.Hu, X.Tang, X.Yang, Y.Ko, T.P.Gao, J.Zheng, Y.Huang, J.W.Yu, Z.Li, L.Han, S.Cai, N.Zhang, Y.Liu, W.Guo, R.T.

(2018) Angew Chem Int Ed Engl 57: 15060-15064

  • DOI: https://doi.org/10.1002/anie.201808231
  • Primary Citation of Related Structures:  
    5YVK, 5YVL, 5YVP, 5Z53, 5Z54, 5ZFJ, 6A8X, 6A92, 6A98, 6A99, 6A9F, 6ADU

  • PubMed Abstract: 

    Found recently in stignomatales, the Stig cyclases catalyze the Cope rearrangement and intramolecular cyclization to produce complex indole alkaloids. Five crystal structures were solved of subfamily 1 and 2 Stig cyclases, which adopt a β-sandwich fold like the non-catalytic carbohydrate-binding motif. Several complex structures were also determined of indole-based compounds, which are bound to the hydrophobic terminal cavity, where a conserved Asp residue makes an H-bond to the indole N and triggers the acid-catalyzed Cope rearrangement. Through analyzing the enzyme-ligand interactions and mutagenesis experiments, several aromatic residues were found important in catalysis. Apart from a common substrate binding mode and catalytic mechanism, potential subfamily variations that may attribute to the different product specificity are implicated. These results shall expand our scope of enzymology, in particular for further investigation of the biosynthetic Cope rearrangement.


  • Organizational Affiliation

    State Key Laboratory of Biocatalysis and Enzyme Engineering, Hubei Collaborative Innovation Center for Green Transformation of Bio-resources, Environmental Microbial Technology Center of Hubei Province, Hubei Key Laboratory of Industrial Biotechnology, College of Life Sciences, Hubei University, Wuhan, 430062, China.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
aromatic prenyltransferase
A, B, C, D
223Mastigocladus laminosus UTEX LB 1931Mutation(s): 0 
Gene Names: fisC
UniProt
Find proteins for A0A1P8VSL7 (Fischerella sp. SAG 46.79)
Explore A0A1P8VSL7 
Go to UniProtKB:  A0A1P8VSL7
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A1P8VSL7
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 3 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
9UL
Query on 9UL

Download Ideal Coordinates CCD File 
E [auth A],
F [auth A],
J [auth B],
K [auth B],
O [auth C]
(3~{Z})-3-(1-methylpyrrolidin-2-ylidene)indole
C13 H14 N2
HNNADWWHLOZSTI-ACCUITESSA-N
CA
Query on CA

Download Ideal Coordinates CCD File 
G [auth A]
H [auth A]
L [auth B]
M [auth B]
P [auth C]
CALCIUM ION
Ca
BHPQYMZQTOCNFJ-UHFFFAOYSA-N
MG
Query on MG

Download Ideal Coordinates CCD File 
I [auth A],
N [auth B],
T [auth D]
MAGNESIUM ION
Mg
JLVVSXFLKOJNIY-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.29 Å
  • R-Value Free: 0.241 
  • R-Value Work: 0.187 
  • R-Value Observed: 0.190 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 70.454α = 90
b = 82.398β = 90
c = 136.575γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
HKL-2000data scaling
PDB_EXTRACTdata extraction
HKL-2000data reduction
PHASERphasing

Structure Validation

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Ligand Structure Quality Assessment 

Created with Raphaël 2.3.0Worse 01 BetterLigand structure goodness of fit to experimental dataBest fitted 9ULClick on this verticalbar to view details

Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2018-12-19
    Type: Initial release
  • Version 1.1: 2018-12-26
    Changes: Data collection, Structure summary
  • Version 1.2: 2023-11-22
    Changes: Data collection, Database references, Derived calculations, Refinement description