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PDBsum entry 4xau

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protein ligands Protein-protein interface(s) links
Transferase PDB id
4xau

 

 

 

 

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Contents
Protein chains
(+ 1 more) 372 a.a.
Ligands
PLP
Waters ×252
PDB id:
4xau
Name: Transferase
Title: Crystal structure of ats13 from actinomadura melliaura
Structure: Putative aminotransferase. Chain: a, b, c, d, e, f, g. Engineered: yes
Source: Actinomadura melliaura. Organism_taxid: 360723. Gene: ats13. Expressed in: escherichia coli 'bl21-gold(de3)plyss ag'. Expression_system_taxid: 866768
Resolution:
3.00Å     R-factor:   0.188     R-free:   0.220
Authors: F.Wang,S.Singh,W.Xu,J.S.Thorson,G.N.Phillips Jr.,Enzyme Discovery For Natural Product Biosynthesis (Natpro)
Key ref: S.Singh et al. (2015). Structural characterization of AtmS13, a putative sugar aminotransferase involved in indolocarbazole AT2433 aminopentose biosynthesis. Proteins, 83, 1547-1554. PubMed id: 26061967 DOI: 10.1002/prot.24844
Date:
15-Dec-14     Release date:   24-Dec-14    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q0H2X1  (Q0H2X1_9ACTN) -  Putative aminotransferase from Actinomadura melliaura
Seq:
Struc:
369 a.a.
372 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1002/prot.24844 Proteins 83:1547-1554 (2015)
PubMed id: 26061967  
 
 
Structural characterization of AtmS13, a putative sugar aminotransferase involved in indolocarbazole AT2433 aminopentose biosynthesis.
S.Singh, Y.Kim, F.Wang, L.Bigelow, M.Endres, M.K.Kharel, G.Babnigg, C.A.Bingman, A.Joachimiak, J.S.Thorson, G.N.Phillips.
 
  ABSTRACT  
 
AT2433 from Actinomadura melliaura is an indolocarbazole antitumor antibiotic structurally distinguished by its unique aminodideoxypentose-containing disaccharide moiety. The corresponding sugar nucleotide-based biosynthetic pathway for this unusual sugar derives from comparative genomics where AtmS13 has been suggested as the contributing sugar aminotransferase (SAT). Determination of the AtmS13 X-ray structure at 1.50-Å resolution reveals it as a member of the aspartate aminotransferase fold type I (AAT-I). Structural comparisons of AtmS13 with homologous SATs that act upon similar substrates implicate potential active site residues that contribute to distinctions in sugar C5 (hexose vs. pentose) and/or sugar C2 (deoxy vs. hydroxyl) substrate specificity. Proteins 2015; 83:1547-1554. © 2015 Wiley Periodicals, Inc.
 

 

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