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PDBsum entry 1kut

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protein Protein-protein interface(s) links
Structural genomics, ligase PDB id
1kut

 

 

 

 

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Contents
Protein chains
213 a.a. *
222 a.a. *
Waters ×81
* Residue conservation analysis
PDB id:
1kut
Name: Structural genomics, ligase
Title: Structural genomics, protein tm1243, (saicar synthetase)
Structure: Phosphoribosylaminoimidazole-succinocarboxamide synthase. Chain: a, b. Synonym: saicar synthetase. Engineered: yes
Source: Thermotoga maritima. Organism_taxid: 2336. Gene: tm1243. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Biol. unit: Dimer (from PQS)
Resolution:
2.20Å     R-factor:   0.245     R-free:   0.281
Authors: R.Zhang,T.Skarina,S.Beasley,A.Edwards,A.Joachimiak,A.Savchenko, Midwest Center For Structural Genomics (Mcsg)
Key ref:
R.Zhang et al. (2006). Structure of SAICAR synthase from Thermotoga maritima at 2.2 angstroms reveals an unusual covalent dimer. Acta Crystallograph Sect F Struct Biol Cryst Commun, 62, 335-339. PubMed id: 16582479 DOI: 10.1107/S1744309106009651
Date:
22-Jan-02     Release date:   14-Aug-02    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9X0X0  (PUR7_THEMA) -  Phosphoribosylaminoimidazole-succinocarboxamide synthase from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
Seq:
Struc:
230 a.a.
213 a.a.
Protein chain
Pfam   ArchSchema ?
Q9X0X0  (PUR7_THEMA) -  Phosphoribosylaminoimidazole-succinocarboxamide synthase from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
Seq:
Struc:
230 a.a.
222 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains A, B: E.C.6.3.2.6  - phosphoribosylaminoimidazolesuccinocarboxamide synthase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Purine Biosynthesis (late stages)
      Reaction: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate + ATP = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4- carboxamido]succinate + ADP + phosphate + 2 H+
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
+ L-aspartate
+ ATP
= (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4- carboxamido]succinate
+ ADP
+ phosphate
+ 2 × H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1107/S1744309106009651 Acta Crystallograph Sect F Struct Biol Cryst Commun 62:335-339 (2006)
PubMed id: 16582479  
 
 
Structure of SAICAR synthase from Thermotoga maritima at 2.2 angstroms reveals an unusual covalent dimer.
R.Zhang, T.Skarina, E.Evdokimova, A.Edwards, A.Savchenko, R.Laskowski, M.E.Cuff, A.Joachimiak.
 
  ABSTRACT  
 
As a part of a structural genomics program, the 2.2 angstroms resolution crystal structure of the PurC gene product from Thermotoga maritima has been solved. This 26.2 kDa protein belongs to the phophoribosylaminoimidazole-succinocarboxamide or SAICAR synthase family of enzymes, the members of which are involved in de novo purine biosynthesis. SAICAR synthase can be divided into three subdomains: two alpha+beta regions exhibiting structural homology with ATP-binding proteins and a carboxy-terminal subdomain of two alpha-helices. The asymmetric unit contains two copies of the protein which are covalently linked by a disulfide bond between Cys126(A) and Cys126(B). This 230-amino-acid protein exhibits high structural homology with SAICAR synthase from baker's yeast. The protein structure is described and compared with that of the ATP-SAICAR synthase complex from yeast.
 
  Selected figure(s)  
 
Figure 1.
Figure 1 Ribbon schematic of the T. maritima SAICAR synthase monomer. The peptide chain is colored blue to red from the N- to the C-terminus. Conserved residue Glu172 is labeled E172; Cys126 is labeled C126 and is cross-linked to its counterpart in the second molecule of the asymmetric unit. All ribbon figures were generated using PyMOL (DeLano, 2002[DeLano, W. L. (2002). The PyMOL Molecular Graphics System. http://www.pymol.org .]).
Figure 3.
Figure 3 Dimeric SAICAR synthase. The covalent dimer is pictured here in stereo with one peptide chain in red and the other in blue. The amino-termini are labeled N and the carboxy-termini are labeled C. The disulfide bridge is located across a (noncrystallographic) twofold axis and is shown as yellow sticks.
 
  The above figures are reprinted from an Open Access publication published by the IUCr: Acta Crystallograph Sect F Struct Biol Cryst Commun (2006, 62, 335-339) copyright 2006.  
  Figures were selected by an automated process.  

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
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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