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PDBsum entry 1cg0
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Ligase PDB id
1cg0

 

 

 

 

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Contents
Protein chain
431 a.a. *
Ligands
HDA
IMO
GDP
Metals
_MG
Waters ×200
* Residue conservation analysis
PDB id:
1cg0
Name: Ligase
Title: Structure of adenylosuccinate synthetase from e. Coli complexed with hadacidin, gdp, 6-phosphoryl-imp, and mg2+
Structure: Protein (adenylosuccinate synthetase). Chain: a. Synonym: ampsase. Engineered: yes
Source: Escherichia coli k12. Organism_taxid: 83333. Strain: k-12. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Homo-Dimer (from PDB file)
Resolution:
2.50Å     R-factor:   0.160     R-free:   0.259
Authors: J.Y.Choe,B.W.Poland,H.Fromm,R.Honzatko
Key ref:
J.Y.Choe et al. (1999). Mechanistic implications from crystalline complexes of wild-type and mutant adenylosuccinate synthetases from Escherichia coli. Biochemistry, 38, 6953-6961. PubMed id: 10346917 DOI: 10.1021/bi990159s
Date:
26-Mar-99     Release date:   17-Jun-99    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P0A7D4  (PURA_ECOLI) -  Adenylosuccinate synthetase from Escherichia coli (strain K12)
Seq:
Struc: 		432 a.a.
431 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.6.3.4.4  - adenylosuccinate synthase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway: 		AMP and GMP Biosynthesis
      Reaction: IMP + L-aspartate + GTP = N6-(1,2-dicarboxyethyl)-AMP + GDP + phosphate + 2 H+
IMP
 +
L-aspartate
Bound ligand (Het Group name = IMO)
matches with 85.19% similarity 		+
GTP
Bound ligand (Het Group name = HDA)
matches with 41.67% similarity 		=
N(6)-(1,2-dicarboxyethyl)-AMP
Bound ligand (Het Group name = GDP)
corresponds exactly 		+ GDP
 + phosphate
 + 2 × H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1021/bi990159s Biochemistry 38:6953-6961 (1999)
PubMed id: 10346917  
 
 
Mechanistic implications from crystalline complexes of wild-type and mutant adenylosuccinate synthetases from Escherichia coli.
J.Y.Choe, B.W.Poland, H.J.Fromm, R.B.Honzatko.
 
  ABSTRACT  
 
Asp13 and His41 are essential residues of adenylosuccinate synthetase, putatively catalyzing the formation of adenylosuccinate from an intermediate of 6-phosphoryl-IMP. Wild-type adenylosuccinate synthetase and three mutant synthetases (Arg143 --> Leu, Lys16 --> Gln, and Arg303 --> Leu) from Eschericha coli have been crystallized in the presence of IMP, hadacidin (an analogue of L-aspartate), Mg2+, and GTP. The active site of each complex contains 6-phosphoryl-IMP, Mg2+, GDP, and hadacidin, except for the Arg303 --> Leu mutant, which does not bind hadacidin. In response to the formation of 6-phosphoryl-IMP, Asp13 enters the inner coordination sphere of the active site Mg2+. His41 hydrogen bonds with 6-phosphoryl-IMP, except in the Arg303 --> Leu complex, where it remains bound to the guanine nucleotide. Hence, recognition of the active site Mg2+ by Asp13 evidently occurs after the formation of 6-phosphoryl-IMP, but recognition of the intermediate by His41 may require the association of L-aspartate with the active site. Structures reported here support a mechanism in which Asp13 and His41 act as the catalytic base and acid, respectively, in the formation of 6-phosphoryl-IMP, and then act together as catalytic acids in the subsequent formation of adenylosuccinate.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
16687397 N.D.Ginder, D.J.Binkowski, H.J.Fromm, and R.B.Honzatko (2006).
Nucleotide complexes of Escherichia coli phosphoribosylaminoimidazole succinocarboxamide synthetase.
  J Biol Chem, 281, 20680-20688.
PDB codes: 2gqr 2gqs
15786719 H.Sun, N.Li, X.Wang, T.Chen, L.Shi, L.Zhang, J.Wang, T.Wan, and X.Cao (2005).
Molecular cloning and characterization of a novel muscle adenylosuccinate synthetase, AdSSL1, from human bone marrow stromal cells.
  Mol Cell Biochem, 269, 85-94.  
12482871 T.Borza, C.V.Iancu, E.Pike, R.B.Honzatko, and H.J.Fromm (2003).
Variations in the response of mouse isozymes of adenylosuccinate synthetase to inhibitors of physiological relevance.
  J Biol Chem, 278, 6673-6679.  
11781326 A.Gorrell, W.Wang, E.Underbakke, Z.Hou, R.B.Honzatko, and H.J.Fromm (2002).
Determinants of L-aspartate and IMP recognition in Escherichia coli adenylosuccinate synthetase.
  J Biol Chem, 277, 8817-8821.  
12004071 C.V.Iancu, T.Borza, H.J.Fromm, and R.B.Honzatko (2002).
IMP, GTP, and 6-phosphoryl-IMP complexes of recombinant mouse muscle adenylosuccinate synthetase.
  J Biol Chem, 277, 26779-26787.
PDB codes: 1iwe 1lny 1lon 1loo
12186864 C.V.Iancu, T.Borza, H.J.Fromm, and R.B.Honzatko (2002).
Feedback inhibition and product complexes of recombinant mouse muscle adenylosuccinate synthetase.
  J Biol Chem, 277, 40536-40543.
PDB codes: 1mez 1mf0 1mf1
11560929 C.V.Iancu, T.Borza, J.Y.Choe, H.J.Fromm, and R.B.Honzatko (2001).
Recombinant mouse muscle adenylosuccinate synthetase: overexpression, kinetics, and crystal structure.
  J Biol Chem, 276, 42146-42152.
PDB code: 1j4b
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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