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Hydrolase PDB-id
2jf6
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Protein chains
464 a.a. *
Ligands
S55 ×2
Waters ×77

* Residue conservation analysis
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PDB id: 2jf6
Name: Hydrolase
Title: Structure of inactive mutant of strictosidine glucosidase in complex with strictosidine

Structure:
Strictosidine-o-beta-d-glucosidase. Chain: a, b. Synonym: strictosidine glucosidase. Engineered: yes

Source:
Rauvolfia serpentina. Serpentwood. Organism_taxid: 4060. Expressed in: escherichia coli. Expression_system_taxid: 562.

UniProt:
Chains A, B: Q8GU20 (Q8GU20_RAUSE)
Pfam  
Seq:
Struc:
Seq:
Struc:
Seq: 532 a.a.
Struc: 464 a.a.
Key:    PfamA domain
 Secondary structure  CATH domain

Resolution:
2.82Å

R-factor:
0.225

R-free:
0.280

Authors:
L.Barleben,S.Panjikar,M.Ruppert,J.Koepke,J.Stockigt

Key ref:
L.Barleben et al. (2007). Molecular architecture of strictosidine glucosidase: the gateway to the biosynthesis of the monoterpenoid indole alkaloid family.. Plant Cell, 19, 2886-2897. [PubMed id: 17890378] [DOI: 10.1105/tpc.106.045682]

Date:
26-Jan-07

Release date:
05-Feb-08

Related entries:
2jf7 structure of strictosidine glucosidase
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    Key reference    
 
 
DOI no: 10.1105/tpc.106.045682 Plant Cell 19:2886-2897 (2007)
PubMed id: 17890378  
 
 
Molecular architecture of strictosidine glucosidase: the gateway to the biosynthesis of the monoterpenoid indole alkaloid family.
L.Barleben, S.Panjikar, M.Ruppert, J.Koepke, J.Stöckigt.
 
  ABSTRACT  
 
Strictosidine beta-D-glucosidase (SG) follows strictosidine synthase (STR1) in the production of the reactive intermediate required for the formation of the large family of monoterpenoid indole alkaloids in plants. This family is composed of approximately 2000 structurally diverse compounds. SG plays an important role in the plant cell by activating the glucoside strictosidine and allowing it to enter the multiple indole alkaloid pathways. Here, we report detailed three-dimensional information describing both native SG and the complex of its inactive mutant Glu207Gln with the substrate strictosidine, thus providing a structural characterization of substrate binding and identifying the amino acids that occupy the active site surface of the enzyme. Structural analysis and site-directed mutagenesis experiments demonstrate the essential role of Glu-207, Glu-416, His-161, and Trp-388 in catalysis. Comparison of the catalytic pocket of SG with that of other plant glucosidases demonstrates the structural importance of Trp-388. Compared with all other glucosidases of plant, bacterial, and archaeal origin, SG's residue Trp-388 is present in a unique structural conformation that is specific to the SG enzyme. In addition to STR1 and vinorine synthase, SG represents the third structural example of enzymes participating in the biosynthetic pathway of the Rauvolfia alkaloid ajmaline. The data presented here will contribute to deciphering the structure and reaction mechanism of other higher plant glucosidases.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
18251710 J.Ziegler, and P.J.Facchini (2008).
Alkaloid biosynthesis: metabolism and trafficking.
  Annu Rev Plant Biol, 59, 735-769.  
18476877 P.J.Facchini, and V.De Luca (2008).
Opium poppy and Madagascar periwinkle: model non-model systems to investigate alkaloid biosynthesis in plants.
  Plant J, 54, 763-784.  
18033585 J.Stöckigt, and S.Panjikar (2007).
Structural biology in plant natural product biosynthesis--architecture of enzymes from monoterpenoid indole and tropane alkaloid biosynthesis.
  Nat Prod Rep, 24, 1382-1400.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.