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PDBsum entry 1m4n

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protein ligands links
Lyase PDB id
1m4n
Jmol
Contents
Protein chain
421 a.a. *
Ligands
PLP-AAD
MES
Waters ×288
* Residue conservation analysis
PDB id:
1m4n
Name: Lyase
Title: Crystal structure of apple acc synthase in complex with [2-( oxy)ethyl](5'-deoxyadenosin-5'-yl)(methyl)sulfonium
Structure: 1-aminocyclopropane-1-carboxylate synthase. Chain: a. Fragment: residues 1-435. Synonym: acc synthase. Engineered: yes
Source: Malus x domestica. Organism_taxid: 3750. Tissue: fruit cortical. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Biol. unit: Dimer (from PDB file)
Resolution:
2.01Å     R-factor:   0.199     R-free:   0.232
Authors: G.Capitani,A.C.Eliot,H.Gut,R.M.Khomutov,J.F.Kirsch,M.G.Grutt
Key ref: G.Capitani et al. (2003). Structure of 1-aminocyclopropane-1-carboxylate synthase in complex with an amino-oxy analogue of the substrate: implications for substrate binding. Biochim Biophys Acta, 1647, 55-60. PubMed id: 12686108 DOI: 10.1016/S1570-9639(03)00049-9
Date:
03-Jul-02     Release date:   22-Apr-03    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P37821  (1A1C_MALDO) -  1-aminocyclopropane-1-carboxylate synthase
Seq:
Struc:
473 a.a.
421 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 6 residue positions (black crosses)

 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
Bound ligand (Het Group name = AAD)
matches with 83.33% similarity
      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   4 terms 
  Biochemical function     catalytic activity     5 terms  

 

 
    reference    
 
 
DOI no: 10.1016/S1570-9639(03)00049-9 Biochim Biophys Acta 1647:55-60 (2003)
PubMed id: 12686108  
 
 
Structure of 1-aminocyclopropane-1-carboxylate synthase in complex with an amino-oxy analogue of the substrate: implications for substrate binding.
G.Capitani, A.C.Eliot, H.Gut, R.M.Khomutov, J.F.Kirsch, M.G.Grütter.
 
  ABSTRACT  
 
The crystal structure of 1-aminocyclopropane-1-carboxylate (ACC) synthase in complex with the substrate analogue [2-(amino-oxy)ethyl](5'-deoxyadenosin-5'-yl)(methyl)sulfonium (AMA) was determined at 2.01-A resolution. The crystallographic results show that a covalent adduct (oxime) is formed between AMA (an amino-oxy analogue of the natural substrate S-adenosyl-L-methionine (SAM)) and the pyridoxal 5'-phosphate (PLP) cofactor of ACC synthase. The oxime formation is supported by spectroscopic data. The ACC synthase-AMA structure provides reliable and detailed information on the binding mode of the natural substrate of ACC synthase and complements previous structural and functional work on this enzyme.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19997759 M.A.Khomutov, S.Mandal, J.Weisell, N.Saxena, A.R.Simonian, J.Vepsalainen, R.Madhubala, and S.N.Kochetkov (2010).
Novel convenient synthesis of biologically active esters of hydroxylamine.
  Amino Acids, 38, 509-517.  
16225687 P.Z.Kozbial, and A.R.Mushegian (2005).
Natural history of S-adenosylmethionine-binding proteins.
  BMC Struct Biol, 5, 19.  
15189147 A.C.Eliot, and J.F.Kirsch (2004).
Pyridoxal phosphate enzymes: mechanistic, structural, and evolutionary considerations.
  Annu Rev Biochem, 73, 383-415.  
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.