PDBsum entry 2h0r

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protein metals Protein-protein interface(s) links
Hydrolase PDB id
Protein chains
(+ 1 more) 216 a.a. *
_ZN ×7
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Structure of the yeast nicotinamidase pnc1p
Structure: Nicotinamidase. Chain: a, b, c, d, e, f, g. Synonym: nicotine deamidase, namase. Ec:
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Strain: mmyo11
2.90Å     R-factor:   0.191     R-free:   0.220
Authors: A.B.Taylor,G.Hu,P.J.Hart,L.Mcalister-Henn
Key ref: G.Hu et al. (2007). Crystal structure of the yeast nicotinamidase Pnc1p. Arch Biochem Biophys, 461, 66-75. PubMed id: 17382284
15-May-06     Release date:   27-Mar-07    
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Protein chains
Pfam   ArchSchema ?
P53184  (PNC1_YEAST) -  Nicotinamidase
216 a.a.
216 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Nicotinamidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Nicotinamide + H2O = nicotinate + NH3
+ H(2)O
= nicotinate
+ NH(3)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   3 terms 
  Biological process     metabolic process   6 terms 
  Biochemical function     catalytic activity     4 terms  


    Added reference    
Arch Biochem Biophys 461:66-75 (2007)
PubMed id: 17382284  
Crystal structure of the yeast nicotinamidase Pnc1p.
G.Hu, A.B.Taylor, L.McAlister-Henn, P.J.Hart.
The yeast nicotinamidase Pnc1p acts in transcriptional silencing by reducing levels of nicotinamide, an inhibitor of the histone deacetylase Sir2p. The Pnc1p structure was determined at 2.9A resolution using MAD and MIRAS phasing methods after inadvertent crystallization during the pursuit of the structure of histidine-tagged yeast isocitrate dehydrogenase (IDH). Pnc1p displays a cluster of surface histidine residues likely responsible for its co-fractionation with IDH from Ni(2+)-coupled chromatography resins. Researchers expressing histidine-tagged proteins in yeast should be aware of the propensity of Pnc1p to crystallize, even when overwhelmed in concentration by the protein of interest. The protein assembles into extended helical arrays interwoven to form an unusually robust, yet porous superstructure. Comparison of the Pnc1p structure with those of three homologous bacterial proteins reveals a common core fold punctuated by amino acid insertions unique to each protein. These insertions mediate the self-interactions that define the distinct higher order oligomeric states attained by these molecules. Pnc1p also acts on pyrazinamide, a substrate analog converted by the nicotinamidase from Mycobacterium tuberculosis into a product toxic to that organism. However, we find no evidence for detrimental effects of the drug on yeast cell growth.

Literature references that cite this PDB file's key reference

  PubMed id Reference
19932181 H.B.Luo, H.Zheng, M.D.Zimmerman, M.Chruszcz, T.Skarina, O.Egorova, A.Savchenko, A.M.Edwards, and W.Minor (2010).
Crystal structure and molecular modeling study of N-carbamoylsarcosine amidase Ta0454 from Thermoplasma acidophilum.
  J Struct Biol, 169, 304-311.
PDB code: 3eef
19846558 K.L.Bogan, C.Evans, P.Belenky, P.Song, C.F.Burant, R.Kennedy, and C.Brenner (2009).
Identification of Isn1 and Sdt1 as glucose- and vitamin-regulated nicotinamide mononucleotide and nicotinic acid mononucleotide [corrected] 5'-nucleotidases responsible for production of nicotinamide riboside and nicotinic acid riboside.
  J Biol Chem, 284, 34861-34869.  
19820182 T.L.Vrablik, L.Huang, S.E.Lange, and W.Hanna-Rose (2009).
Nicotinamidase modulation of NAD+ biosynthesis and nicotinamide levels separately affect reproductive development and cell survival in C. elegans.
  Development, 136, 3637-3646.  
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