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PDBsum entry 3kg9

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protein Protein-protein interface(s) links
Lyase PDB id
3kg9
Jmol
Contents
Protein chains
281 a.a. *
Waters ×502
* Residue conservation analysis
PDB id:
3kg9
Name: Lyase
Title: Dehydratase domain from curk module of curacin polyketide sy
Structure: Curk. Chain: a, b. Fragment: dehydratase domain, residues 958-1250. Engineered: yes
Source: Lyngbya majuscula. Organism_taxid: 158786. Gene: curk. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.70Å     R-factor:   0.184     R-free:   0.217
Authors: D.L.Akey,J.L.Smith
Key ref: D.L.Akey et al. (2010). Crystal structures of dehydratase domains from the curacin polyketide biosynthetic pathway. Structure, 18, 94-105. PubMed id: 20152156
Date:
28-Oct-09     Release date:   19-Jan-10    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q6DNE2  (Q6DNE2_9CYAN) -  CurK
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
2232 a.a.
281 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
Structure 18:94-105 (2010)
PubMed id: 20152156  
 
 
Crystal structures of dehydratase domains from the curacin polyketide biosynthetic pathway.
D.L.Akey, J.R.Razelun, J.Tehranisa, D.H.Sherman, W.H.Gerwick, J.L.Smith.
 
  ABSTRACT  
 
Modular polyketide synthases (PKS) make novel natural products through a series of preprogrammed chemical steps catalyzed by an assembly line of multidomain modules. Each assembly-line step involves unique extension and modification reactions, resulting in tremendous diversity of polyketide products. Dehydratase domains catalyze formation of an alpha,beta-double bond in the nascent polyketide intermediate. We present crystal structures of the four dehydratase domains from the curacin A PKS. The catalytic residues and substrate binding site reside in a tunnel within a single monomer. The positions of the catalytic residues and shape of the substrate tunnel explain how chirality of the substrate hydroxyl group may determine the configuration of the product double bond. Access to the active site may require opening the substrate tunnel, forming an open trench. The arrangement of monomers within the dimer is consistent among PKS dehydratases and differs from that seen in the related mammalian fatty acid synthases.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
  21472957 O.Vergnolle, F.Hahn, A.Baerga-Ortiz, P.F.Leadlay, and J.N.Andexer (2011).
Stereoselectivity of isolated dehydratase domains of the borrelidin polyketide synthase: implications for cis double bond formation.
  Chembiochem, 12, 1011-1014.  
20442916 A.C.Jones, E.A.Monroe, E.B.Eisman, L.Gerwick, D.H.Sherman, and W.H.Gerwick (2010).
The unique mechanistic transformations involved in the biosynthesis of modular natural products from marine cyanobacteria.
  Nat Prod Rep, 27, 1048-1065.  
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