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PDBsum entry 1iax

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protein ligands Protein-protein interface(s) links
Lyase PDB id
1iax
Jmol
Contents
Protein chains
417 a.a. *
Ligands
SO4 ×2
PLP ×2
Waters ×19
* Residue conservation analysis
PDB id:
1iax
Name: Lyase
Title: Crystal structure of acc synthase complexed with plp
Structure: 1-aminocyclopropane-1-carboxylate synthase 2. Chain: a, b. Fragment: residues 11-438. Synonym: acc synthase 2. Engineered: yes
Source: Solanum lycopersicum. Organism_taxid: 4081. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
Biol. unit: Dimer (from PQS)
Resolution:
2.80Å     R-factor:   0.218     R-free:   0.293
Authors: Q.Huai,Y.Xia,Y.Chen,B.Callahan,N.Li,H.Ke
Key ref:
Q.Huai et al. (2001). Crystal structures of 1-aminocyclopropane-1-carboxylate (ACC) synthase in complex with aminoethoxyvinylglycine and pyridoxal-5'-phosphate provide new insight into catalytic mechanisms. J Biol Chem, 276, 38210-38216. PubMed id: 11431475 DOI: 10.1074/jbc.M103840200
Date:
24-Mar-01     Release date:   04-Apr-01    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P18485  (1A12_SOLLC) -  1-aminocyclopropane-1-carboxylate synthase 2
Seq:
Struc:
485 a.a.
417 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.4.4.1.14  - 1-aminocyclopropane-1-carboxylate synthase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Ethylene Biosynthesis
      Reaction: S-adenosyl-L-methionine = 1-aminocyclopropane-1-carboxylate + methylthioadenosine
S-adenosyl-L-methionine
= 1-aminocyclopropane-1-carboxylate
+ methylthioadenosine
      Cofactor: Pyridoxal 5'-phosphate
Pyridoxal 5'-phosphate
Bound ligand (Het Group name = PLP) matches with 93.75% similarity
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     biosynthetic process   1 term 
  Biochemical function     catalytic activity     2 terms  

 

 
    reference    
 
 
DOI no: 10.1074/jbc.M103840200 J Biol Chem 276:38210-38216 (2001)
PubMed id: 11431475  
 
 
Crystal structures of 1-aminocyclopropane-1-carboxylate (ACC) synthase in complex with aminoethoxyvinylglycine and pyridoxal-5'-phosphate provide new insight into catalytic mechanisms.
Q.Huai, Y.Xia, Y.Chen, B.Callahan, N.Li, H.Ke.
 
  ABSTRACT  
 
The structures of tomato 1-aminocyclopropane-1-carboxylate synthase (ACS) in complex with either cofactor pyridoxal-5'-phosphate (PLP) or both PLP and inhibitor aminoethoxyvinylglycine have been determined by x-ray crystallography. The structures showed good conservation of the catalytic residues, suggesting a similar catalytic mechanism for ACS and other PLP-dependent enzymes. However, the proximity of Tyr152 to the C-gamma-S bond of model substrate S-adenosylmethionine implies its critical role in the catalysis. The concerted accomplishment of catalysis by cofactor PLP and a protein residue, as proposed on the basis of the ACS structures in this paper, may represent a general scheme for the diversity of PLP-dependent catalyses. PLP-dependent enzymes have been categorized into four types of folds. A structural comparison revealed that a core fragment of ACS in fold type I is superimposable over tryptophan synthase beta subunit in fold type II and mouse ornithine decarboxylase in fold type III, thus suggesting a divergent evolution of PLP-dependent enzymes.
 
  Selected figure(s)  
 
Figure 4.
Fig. 4. Schematic presentation of PLP and AVG binding at the active site. The dotted lines represent the hydrogen bonds. In three-dimensions, Tyr152 stacks in a parallel manner over the pyridine ring of PLP, and the -amino of AVG is ~4 Å away from the C4' of PLP.
Figure 6.
Fig. 6. The putative mechanism for conversion of SAM to ACC.
 
  The above figures are reprinted by permission from the ASBMB: J Biol Chem (2001, 276, 38210-38216) copyright 2001.  
  Figures were selected by the author.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20689184 S.R.Choudhury, S.K.Singh, S.Roy, and D.N.Sengupta (2010).
An insight into the sequential, structural and phylogenetic properties of banana 1-aminocyclopropane-1-carboxylate synthase 1 and study of its interaction with pyridoxal-5'-phosphate and aminoethoxyvinylglycine.
  J Biosci, 35, 281-294.  
20543073 X.Lee, A.Fox, J.Sufrin, H.Henry, P.Majcherczyk, D.Haas, and C.Reimmann (2010).
Identification of the biosynthetic gene cluster for the Pseudomonas aeruginosa antimetabolite L-2-amino-4-methoxy-trans-3-butenoic acid.
  J Bacteriol, 192, 4251-4255.  
19578542 A.Boualem, C.Troadec, I.Kovalski, M.A.Sari, R.Perl-Treves, and A.Bendahmane (2009).
A conserved ethylene biosynthesis enzyme leads to andromonoecy in two cucumis species.
  PLoS One, 4, e6144.  
15949763 H.S.Chae, and J.J.Kieber (2005).
Eto Brute? Role of ACS turnover in regulating ethylene biosynthesis.
  Trends Plant Sci, 10, 291-296.  
16091151 H.Yoshida, M.Nagata, K.Saito, K.L.Wang, and J.R.Ecker (2005).
Arabidopsis ETO1 specifically interacts with and negatively regulates type 2 1-aminocyclopropane-1-carboxylate synthases.
  BMC Plant Biol, 5, 14.  
16225687 P.Z.Kozbial, and A.R.Mushegian (2005).
Natural history of S-adenosylmethionine-binding proteins.
  BMC Struct Biol, 5, 19.  
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