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PDBsum entry 5o15
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protein ligands Protein-protein interface(s) links
Lyase PDB id
5o15

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
289 a.a.
Ligands
GOL
Waters ×734
PDB id:
5o15
Name: Lyase
Title: Crystal structure of bifunctional dehydratase-cyclase domain in ambruticin biosynthesis
Structure: Ambc. Chain: a, b. Fragment: bifunctional dehydratase-cyclase domain, unp residues 918- 1228. Engineered: yes
Source: Sorangium cellulosum. Organism_taxid: 56. Gene: ambc. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.17Å     R-factor:   0.136     R-free:   0.158
Authors: K.H.Sung,G.Berkhan,T.Hollmann,L.Wagner,F.Hahn,W.Blankenfeldt
Key ref: K.H.Sung et al. (2018). Insights into the Dual Activity of a Bifunctional Dehydratase-Cyclase Domain. Angew Chem Int Ed Engl, 57, 343-347. PubMed id: 29084363 DOI: 10.1002/anie.201707774
Date:
18-May-17     Release date:   08-Nov-17    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
A1YBQ4  (A1YBQ4_SORCE) -  AmbC from Sorangium cellulosum
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		3655 a.a.
289 a.a.
Key:    PfamA domain  Secondary structure

 

 
DOI no: 10.1002/anie.201707774 Angew Chem Int Ed Engl 57:343-347 (2018)
PubMed id: 29084363  
 
 
Insights into the Dual Activity of a Bifunctional Dehydratase-Cyclase Domain.
K.H.Sung, G.Berkhan, T.Hollmann, L.Wagner, W.Blankenfeldt, F.Hahn.
 
  ABSTRACT  
 
Oxygen-containing heterocycles are a common structural motif in polyketide natural products and contribute significantly to their biological activity. Here, we report structural and mechanistic investigations on AmbDH3, a polyketide synthase domain with dual activity as dehydratase (DH) and pyran-forming cyclase in ambruticin biosynthesis. AmbDH3 is similar to monofunctional DH domains, using H51 and D215 for dehydration. V173 was confirmed as a diagnostic residue for cyclization activity by a mutational study and enzymatic in vitro experiments. Similar motifs were observed in the seemingly monofunctional AmbDH2, which also shows an unexpected cyclase activity. Our results pave the way for mining of hidden cyclases in biosynthetic pathways. They also open interesting prospects for the generation of novel biocatalysts for chemoenzymatic synthesis and pyran-polyketides by combinatorial biosynthesis.
 

 

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