PDBsum entry 1mf0

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Ligase PDB id
Protein chain
431 a.a. *
Waters ×107
* Residue conservation analysis
PDB id:
Name: Ligase
Title: Structure of the recombinant mouse-muscle adenylosuccinate s complexed with amp, gdp, hpo4(2-), and mg(2+)
Structure: Adenylosuccinate synthetase. Chain: a. Synonym: adss, ampsase. Engineered: yes
Source: Mus musculus. House mouse. Organism_taxid: 10090. Gene: adss1. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
Biol. unit: Dimer (from PDB file)
2.50Å     R-factor:   0.219     R-free:   0.292
Authors: C.V.Iancu,T.Borza,H.J.Fromm,R.B.Honzatko
Key ref:
C.V.Iancu et al. (2002). Feedback inhibition and product complexes of recombinant mouse muscle adenylosuccinate synthetase. J Biol Chem, 277, 40536-40543. PubMed id: 12186864 DOI: 10.1074/jbc.M204952200
09-Aug-02     Release date:   30-Oct-02    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P28650  (PURA1_MOUSE) -  Adenylosuccinate synthetase isozyme 1
457 a.a.
431 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Adenylosuccinate synthase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

AMP and GMP Biosynthesis
      Reaction: GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)- AMP
+ L-aspartate
Bound ligand (Het Group name = GDP)
corresponds exactly
Bound ligand (Het Group name = PO4)
corresponds exactly
N(6)-(1,2-dicarboxyethyl)- AMP
Bound ligand (Het Group name = AMP)
matches with 74.19% similarity
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   2 terms 
  Biological process     cellular response to drug   12 terms 
  Biochemical function     nucleotide binding     10 terms  


DOI no: 10.1074/jbc.M204952200 J Biol Chem 277:40536-40543 (2002)
PubMed id: 12186864  
Feedback inhibition and product complexes of recombinant mouse muscle adenylosuccinate synthetase.
C.V.Iancu, T.Borza, H.J.Fromm, R.B.Honzatko.
Adenylosuccinate synthetase governs the committed step of AMP biosynthesis, the generation of 6-phosphoryl-IMP from GTP and IMP followed by the formation of adenylosuccinate from 6-phosphoryl-IMP and l-aspartate. The enzyme is subject to feedback inhibition by AMP and adenylosuccinate, but crystallographic complexes of the mouse muscle synthetase presented here infer mechanisms of inhibition that involve potentially synergistic ligand combinations. AMP alone adopts the productive binding mode of IMP and yet stabilizes the active site in a conformation that favors the binding of Mg(2+)-IMP to the GTP pocket. On the other hand, AMP, in the presence of GDP, orthophosphate, and Mg(2+), adopts the binding mode of adenylosuccinate. Depending on circumstances then, AMP behaves as an analogue of IMP or as an analogue of adenylosuccinate. The complex of adenylosuccinate.GDP.Mg(2+).sulfate, the first structure of an adenylosuccinate-bound synthetase, reveals significant geometric distortions and tight nonbonded contacts relevant to the proposed catalytic mechanism. Adenylosuccinate forms from 6-phosphoryl-IMP and l-aspartate by the movement of the purine ring into the alpha-amino group of l-aspartate.
  Selected figure(s)  
Figure 2.
Fig. 2. Stereoview of AMP bound to the active site. Electron density is from an omit map (coefficients of 2F[obs] F[calc], [calc] phases) contoured at 3 using a cut-off radius of 1 Å. Dashed lines represent donor-acceptor interactions.
Figure 4.
Fig. 4. Stereoview of SAMP-product complex. Electron density covering SAMP is from an omit map (coefficients of 2 F[obs] F[calc], [calc] phases) contoured at 3 using a cut-off radius of 1 Å. Dashed lines represent donor-acceptor interactions and coordinate bonds to the Mg2+.
  The above figures are reprinted by permission from the ASBMB: J Biol Chem (2002, 277, 40536-40543) copyright 2002.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
16216072 J.A.Endrizzi, H.Kim, P.M.Anderson, and E.P.Baldwin (2005).
Mechanisms of product feedback regulation and drug resistance in cytidine triphosphate synthetases from the structure of a CTP-inhibited complex.
  Biochemistry, 44, 13491-13499.
PDB code: 2ad5
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