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PDBsum entry 1zn8

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protein ligands metals Protein-protein interface(s) links
Transferase PDB id
1zn8
Jmol
Contents
Protein chain
178 a.a. *
Ligands
AMP ×2
Metals
_CL
Waters ×355
* Residue conservation analysis
PDB id:
1zn8
Name: Transferase
Title: Human adenine phosphoribosyltransferase complexed with amp, group p1 at 1.76 a resolution
Structure: Adenine phosphoribosyltransferase. Chain: a, b. Synonym: aprt. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: aprt. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Biol. unit: Dimer (from PQS)
Resolution:
1.76Å     R-factor:   0.160     R-free:   0.211
Authors: J.Iulek,M.Silva,C.H.T.P.Tomich,O.H.Thiemann
Key ref: C.H.Silva et al. (2008). Structural complexes of human adenine phosphoribosyltransferase reveal novel features of the APRT catalytic mechanism. J Biomol Struct Dyn, 25, 589-597. PubMed id: 18399692 DOI: 10.1080/07391102.2008.10507205
Date:
11-May-05     Release date:   25-Apr-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P07741  (APT_HUMAN) -  Adenine phosphoribosyltransferase
Seq:
Struc:
180 a.a.
178 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.4.2.7  - Adenine phosphoribosyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Ribose activation
      Reaction: AMP + diphosphate = adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP
Bound ligand (Het Group name = AMP)
corresponds exactly
+ diphosphate
= adenine
+ 5-phospho-alpha-D-ribose 1-diphosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   5 terms 
  Biological process     AMP salvage   11 terms 
  Biochemical function     transferase activity     5 terms  

 

 
    reference    
 
 
DOI no: 10.1080/07391102.2008.10507205 J Biomol Struct Dyn 25:589-597 (2008)
PubMed id: 18399692  
 
 
Structural complexes of human adenine phosphoribosyltransferase reveal novel features of the APRT catalytic mechanism.
C.H.Silva, M.Silva, J.Iulek, O.H.Thiemann.
 
  ABSTRACT  
 
Adenine phosphoribosyltransferase (APRT) is an important enzyme component of the purine recycling pathway. Parasitic protozoa of the order Kinetoplastida are unable to synthesize purines de novo and use the salvage pathway for the synthesis of purine bases rendering this biosynthetic pathway an attractive target for antiparasitic drug design. The recombinant human adenine phosphoribosyltransferase (hAPRT) structure was resolved in the presence of AMP in the active site to 1.76 A resolution and with the substrates PRPP and adenine simultaneously bound to the catalytic site to 1.83 A resolution. An additional structure was solved containing one subunit of the dimer in the apo-form to 2.10 A resolution. Comparisons of these three hAPRT structures with other 'type I' PRTases revealed several important features of this class of enzymes. Our data indicate that the flexible loop structure adopts an open conformation before and after binding of both substrates adenine and PRPP. Comparative analyses presented here provide structural evidence to propose the role of Glu104 as the residue that abstracts the proton of adenine N9 atom before its nucleophilic attack on the PRPP anomeric carbon. This work leads to new insights to the understanding of the APRT catalytic mechanism.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20105085 Y.Cui, C.S.Piao, K.C.Ha, D.S.Kim, G.H.Lee, H.K.Kim, S.W.Chae, Y.C.Lee, S.J.Park, W.H.Yoo, H.R.Kim, and H.J.Chae (2010).
Measuring adriamycin-induced cardiac hemodynamic dysfunction with a proteomics approach.
  Immunopharmacol Immunotoxicol, 32, 376-386.  
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