spacer
spacer

PDBsum entry 1b8g

Go to PDB code: 
protein ligands Protein-protein interface(s) links
Lyase PDB id
1b8g
Jmol
Contents
Protein chains
421 a.a. *
Ligands
PLP ×2
Waters ×174
* Residue conservation analysis
PDB id:
1b8g
Name: Lyase
Title: 1-aminocyclopropane-1-carboxylate synthase
Structure: Protein (1-aminocyclopropane-1-carboxylate syntha chain: a, b. Synonym: acc synthase, s-adenosyl-l-methionine methylthioad lyase. Engineered: yes
Source: Malus x domestica. Organism_taxid: 3750. Tissue: fruit cortical tissue. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Dimer (from PQS)
Resolution:
2.37Å     R-factor:   0.179     R-free:   0.242
Authors: G.Capitani,E.Hohenester,L.Feng,P.Storici,J.F.Kirsch,J.N.Jans
Key ref:
G.Capitani et al. (1999). Structure of 1-aminocyclopropane-1-carboxylate synthase, a key enzyme in the biosynthesis of the plant hormone ethylene. J Mol Biol, 294, 745-756. PubMed id: 10610793 DOI: 10.1006/jmbi.1999.3255
Date:
31-Jan-99     Release date:   26-Jan-00    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
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

 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   4 terms 
  Biochemical function     catalytic activity     5 terms  

 

 
    reference    
 
 
DOI no: 10.1006/jmbi.1999.3255 J Mol Biol 294:745-756 (1999)
PubMed id: 10610793  
 
 
Structure of 1-aminocyclopropane-1-carboxylate synthase, a key enzyme in the biosynthesis of the plant hormone ethylene.
G.Capitani, E.Hohenester, L.Feng, P.Storici, J.F.Kirsch, J.N.Jansonius.
 
  ABSTRACT  
 
The 2.4 A crystal structure of the vitamin B6-dependent enzyme 1-aminocyclopropane-1-carboxylate (ACC) synthase is described. This enzyme catalyses the committed step in the biosynthesis of ethylene, a plant hormone that is responsible for the initiation of fruit ripening and for regulating many other developmental processes. ACC synthase has 15 % sequence identity with the well-studied aspartate aminotransferase, and a completely different catalytic activity yet the overall folds and the active sites are very similar. The new structure together with available biochemical data enables a comparative mechanistic analysis that largely explains the catalytic roles of the conserved and non-conserved active site residues. An external aldimine reaction intermediate (external aldimine with ACC, i.e. with the product) has been modeled. The new structure provides a basis for the rational design of inhibitors with broad agricultural applications.
 
  Selected figure(s)  
 
Figure 3.
Figure 3. Active site views of ACC synthase. (a) Stereo view of the ACC synthase active site with the most import- ant residues labeled (prepared with the program O (Jones & Kjeldgaard, 1991)). Residues within a sphere of 11 Å of the cofactor are depicted in yellow and atom colors, and shown in each two alternative conformation. Tyr85, which is contributed by the neighboring subunit, is labeled with an asterisk. (b) Detailed stereo view of the ACC synthase active site (subunit B), showing the covalent linkage between the cofactor and Lys273. The final 2Fo - Fc map, con- toured at 1.2s, is superimposed on the atomic model. The model is depicted in yellow and atom colors. The unde- fined additional density in front of the cofactor and modeled as three water molecules (red spheres) is visible at the top right. Prepared with O.
Figure 4.
Figure 4. Stereo view of the superposition of the ACC synthase and AATase active sites. Residues within 11 Å of the cofactors are shown. ACC synthase is depicted in yellow, AATase in green. Residue labels for ACC synthase appear in gold, those for AATase residues in black. Tyr85 (ACC synthase) and Tyr70 and Arg292 (AATase) are con- tributed by the neighboring subunit and are labeled with an asterisk. Prepared with O.
 
  The above figures are reprinted by permission from Elsevier: J Mol Biol (1999, 294, 745-756) copyright 1999.  
  Figures were selected by an automated process.  

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.  
19752216 A.Tsuchisaka, G.Yu, H.Jin, J.M.Alonso, J.R.Ecker, X.Zhang, S.Gao, and A.Theologis (2009).
A combinatorial interplay among the 1-aminocyclopropane-1-carboxylate isoforms regulates ethylene biosynthesis in Arabidopsis thaliana.
  Genetics, 183, 979.  
19567479 Z.Lin, S.Zhong, and D.Grierson (2009).
Recent advances in ethylene research.
  J Exp Bot, 60, 3311-3336.  
18535295 I.El-Sharkawy, W.S.Kim, S.Jayasankar, A.M.Svircev, and D.C.Brown (2008).
Differential regulation of four members of the ACC synthase gene family in plum.
  J Exp Bot, 59, 2009-2027.  
17566975 R.Pedreschi, E.Vanstreels, S.Carpentier, M.Hertog, J.Lammertyn, J.Robben, J.P.Noben, R.Swennen, J.Vanderleyden, and B.M.Nicolaï (2007).
Proteomic analysis of core breakdown disorder in Conference pears (Pyrus communis L.).
  Proteomics, 7, 2083-2099.  
16640556 S.Sivaraman, and J.F.Kirsch (2006).
The narrow substrate specificity of human tyrosine aminotransferase--the enzyme deficient in tyrosinemia type II.
  FEBS J, 273, 1920-1929.  
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.  
14983000 A.Tsuchisaka, and A.Theologis (2004).
Heterodimeric interactions among the 1-amino-cyclopropane-1-carboxylate synthase polypeptides encoded by the Arabidopsis gene family.
  Proc Natl Acad Sci U S A, 101, 2275-2280.  
15118728 K.L.Wang, H.Yoshida, C.Lurin, and J.R.Ecker (2004).
Regulation of ethylene gas biosynthesis by the Arabidopsis ETO1 protein.
  Nature, 428, 945-950.  
15489165 Z.Zhang, J.S.Ren, I.J.Clifton, and C.J.Schofield (2004).
Crystal structure and mechanistic implications of 1-aminocyclopropane-1-carboxylic acid oxidase--the ethylene-forming enzyme.
  Chem Biol, 11, 1383-1394.
PDB codes: 1w9y 1wa6
12968022 T.Yamagami, A.Tsuchisaka, K.Yamada, W.F.Haddon, L.A.Harden, and A.Theologis (2003).
Biochemical diversity among the 1-amino-cyclopropane-1-carboxylate synthase isozymes encoded by the Arabidopsis gene family.
  J Biol Chem, 278, 49102-49112.  
11939774 C.G.Cheong, C.B.Bauer, K.R.Brushaber, J.C.Escalante-Semerena, and I.Rayment (2002).
Three-dimensional structure of the L-threonine-O-3-phosphate decarboxylase (CobD) enzyme from Salmonella enterica.
  Biochemistry, 41, 4798-4808.
PDB codes: 1kus 1lkc
12119022 C.G.Cheong, J.C.Escalante-Semerena, and I.Rayment (2002).
Structural studies of the L-threonine-O-3-phosphate decarboxylase (CobD) enzyme from Salmonella enterica: the apo, substrate, and product-aldimine complexes.
  Biochemistry, 41, 9079-9089.
PDB codes: 1l4b 1l4e 1l4f 1l4g 1l4h 1l4k 1l4l 1l4m 1l4n 1l5f 1l5k 1l5l 1l5m 1l5n 1l5o 1lc5 1lc7 1lc8
12235163 E.B.Kuettner, R.Hilgenfeld, and M.S.Weiss (2002).
The active principle of garlic at atomic resolution.
  J Biol Chem, 277, 46402-46407.
PDB code: 1lk9
12228256 G.Capitani, D.L.McCarthy, H.Gut, M.G.Grütter, and J.F.Kirsch (2002).
Apple 1-aminocyclopropane-1-carboxylate synthase in complex with the inhibitor L-aminoethoxyvinylglycine. Evidence for a ketimine intermediate.
  J Biol Chem, 277, 49735-49742.
PDB code: 1m7y
11752307 Y.Wang, J.B.Anderson, J.Chen, L.Y.Geer, S.He, D.I.Hurwitz, C.A.Liebert, T.Madej, G.H.Marchler, A.Marchler-Bauer, A.R.Panchenko, B.A.Shoemaker, J.S.Song, P.A.Thiessen, R.A.Yamashita, and S.H.Bryant (2002).
MMDB: Entrez's 3D-structure database.
  Nucleic Acids Res, 30, 249-252.  
11294630 K.Haruyama, T.Nakai, I.Miyahara, K.Hirotsu, H.Mizuguchi, H.Hayashi, and H.Kagamiyama (2001).
Structures of Escherichia coli histidinol-phosphate aminotransferase and its complexes with histidinol-phosphate and N-(5'-phosphopyridoxyl)-L-glutamate: double substrate recognition of the enzyme.
  Biochemistry, 40, 4633-4644.
PDB codes: 1gew 1gex 1gey
11515533 Y.Kakuta, T.Igarashi, T.Murakami, H.Ito, H.Matsui, and M.Honma (2001).
1-Aminocyclopropane-1-carboxylate synthase of Penicillium citrinum: primary structure and expression in Escherichia coli and Saccharomyces cerevisiae.
  Biosci Biotechnol Biochem, 65, 1511-1518.  
11031228 A.B.Bleecker, and H.Kende (2000).
Ethylene: a gaseous signal molecule in plants.
  Annu Rev Cell Dev Biol, 16, 1.  
11106504 L.Feng, M.K.Geck, A.C.Eliot, and J.F.Kirsch (2000).
Aminotransferase activity and bioinformatic analysis of 1-aminocyclopropane-1-carboxylate synthase.
  Biochemistry, 39, 15242-15249.  
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.