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PDBsum entry 1xg2

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protein Protein-protein interface(s) links
Hydrolase/hydrolase inhibitor PDB id
1xg2
Jmol
Contents
Protein chains
317 a.a. *
151 a.a. *
Waters ×453
* Residue conservation analysis
PDB id:
1xg2
Name: Hydrolase/hydrolase inhibitor
Title: Crystal structure of the complex between pectin methylesterase and its inhibitor protein
Structure: Pectinesterase 1. Chain: a. Synonym: pectin methylesterase 1, pe 1. Pectinesterase inhibitor. Chain: b. Synonym: pectin methylesterase inhibitor, pmei. Engineered: yes
Source: Solanum lycopersicum. Organism_taxid: 4081. Tissue: pericarp. Actinidia chinensis. Organism_taxid: 3625. Expressed in: pichia pastoris. Expression_system_taxid: 4922.
Biol. unit: Tetramer (from PQS)
Resolution:
1.90Å     R-factor:   0.199     R-free:   0.232
Authors: A.Di Matteo,A.Raiola,L.Camardella,A.Giovane,D.Bonivento, G.De Lorenzo,F.Cervone,D.Bellincampi,D.Tsernoglou
Key ref: A.Di Matteo et al. (2005). Structural basis for the interaction between pectin methylesterase and a specific inhibitor protein. Plant Cell, 17, 849-858. PubMed id: 15722470
Date:
16-Sep-04     Release date:   22-Mar-05    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P14280  (PME1_SOLLC) -  Pectinesterase 1
Seq:
Struc:
 
Seq:
Struc:
546 a.a.
317 a.a.
Protein chain
Pfam   ArchSchema ?
P83326  (PMEI_ACTDE) -  Pectinesterase inhibitor
Seq:
Struc:
185 a.a.
151 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: Chain A: E.C.3.1.1.11  - Pectinesterase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Pectin + n H2O = n methanol + pectate
Pectin
+ n H(2)O
= n methanol
+ pectate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cell wall   2 terms 
  Biological process     metabolic process   3 terms 
  Biochemical function     enzyme inhibitor activity     2 terms  

 

 
    reference    
 
 
Plant Cell 17:849-858 (2005)
PubMed id: 15722470  
 
 
Structural basis for the interaction between pectin methylesterase and a specific inhibitor protein.
A.Di Matteo, A.Giovane, A.Raiola, L.Camardella, D.Bonivento, G.De Lorenzo, F.Cervone, D.Bellincampi, D.Tsernoglou.
 
  ABSTRACT  
 
Pectin, one of the main components of the plant cell wall, is secreted in a highly methyl-esterified form and subsequently deesterified in muro by pectin methylesterases (PMEs). In many developmental processes, PMEs are regulated by either differential expression or posttranslational control by protein inhibitors (PMEIs). PMEIs are typically active against plant PMEs and ineffective against microbial enzymes. Here, we describe the three-dimensional structure of the complex between the most abundant PME isoform from tomato fruit (Lycopersicon esculentum) and PMEI from kiwi (Actinidia deliciosa) at 1.9-A resolution. The enzyme folds into a right-handed parallel beta-helical structure typical of pectic enzymes. The inhibitor is almost all helical, with four long alpha-helices aligned in an antiparallel manner in a classical up-and-down four-helical bundle. The two proteins form a stoichiometric 1:1 complex in which the inhibitor covers the shallow cleft of the enzyme where the putative active site is located. The four-helix bundle of the inhibitor packs roughly perpendicular to the main axis of the parallel beta-helix of PME, and three helices of the bundle interact with the enzyme. The interaction interface displays a polar character, typical of nonobligate complexes formed by soluble proteins. The structure of the complex gives an insight into the specificity of the inhibitor toward plant PMEs and the mechanism of regulation of these enzymes.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21046145 E.Vandevenne, S.Christiaens, S.Van Buggenhout, R.P.Jolie, M.González-Vallinas, T.Duvetter, P.J.Declerck, M.E.Hendrickx, A.Gils, and A.Van Loey (2011).
Advances in understanding pectin methylesterase inhibitor in kiwi fruit: an immunological approach.
  Planta, 233, 287-298.  
20229192 G.Y.Zhang, J.Feng, J.Wu, and X.W.Wang (2010).
BoPMEI1, a pollen-specific pectin methylesterase inhibitor, has an essential role in pollen tube growth.
  Planta, 231, 1323-1334.  
20858733 M.Hothorn, W.Van den Ende, W.Lammens, V.Rybin, and K.Scheffzek (2010).
Structural insights into the pH-controlled targeting of plant cell-wall invertase by a specific inhibitor protein.
  Proc Natl Acad Sci U S A, 107, 17427-17432.
PDB code: 2xqr
20558896 M.J.Hong, D.Y.Kim, T.G.Lee, W.B.Jeon, and Y.W.Seo (2010).
Functional characterization of pectin methylesterase inhibitor (PMEI) in wheat.
  Genes Genet Syst, 85, 97.  
20528916 S.Kumar, N.Singh, M.Sinha, D.Dube, S.B.Singh, A.Bhushan, P.Kaur, A.Srinivasan, S.Sharma, and T.P.Singh (2010).
Crystal structure determination and inhibition studies of a novel xylanase and alpha-amylase inhibitor protein (XAIP) from Scadoxus multiflorus.
  FEBS J, 277, 2868-2882.
PDB codes: 3hu7 3m7s
20080727 V.Lionetti, F.Francocci, S.Ferrari, C.Volpi, D.Bellincampi, R.Galletti, R.D'Ovidio, G.De Lorenzo, and F.Cervone (2010).
Engineering the cell wall by reducing de-methyl-esterified homogalacturonan improves saccharification of plant tissues for bioconversion.
  Proc Natl Acad Sci U S A, 107, 616-621.  
18936961 S.Dedeurwaerder, L.Menu-Bouaouiche, A.Mareck, P.Lerouge, and F.Guerineau (2009).
Activity of an atypical Arabidopsis thaliana pectin methylesterase.
  Planta, 229, 311-321.  
19144003 S.Wolf, T.Rausch, and S.Greiner (2009).
The N-terminal pro region mediates retention of unprocessed type-I PME in the Golgi apparatus.
  Plant J, 58, 361-375.  
18266922 C.Rautengarten, B.Usadel, L.Neumetzler, J.Hartmann, D.Büssis, and T.Altmann (2008).
A subtilisin-like serine protease essential for mucilage release from Arabidopsis seed coats.
  Plant J, 54, 466-480.  
18824396 D.Cantu, A.R.Vicente, J.M.Labavitch, A.B.Bennett, and A.L.Powell (2008).
Strangers in the matrix: plant cell walls and pathogen susceptibility.
  Trends Plant Sci, 13, 610-617.  
17932919 M.A.Ciardiello, R.D'Avino, A.Amoresano, L.Tuppo, A.Carpentieri, V.Carratore, M.Tamburrini, A.Giovane, P.Pucci, and L.Camardella (2008).
The peculiar structural features of kiwi fruit pectin methylesterase: amino acid sequence, oligosaccharides structure, and modeling of the interaction with its natural proteinaceous inhibitor.
  Proteins, 71, 195-206.  
18453640 M.González-Agüero, L.Pavez, F.Ibáñez, I.Pacheco, R.Campos-Vargas, L.A.Meisel, A.Orellana, J.Retamales, H.Silva, M.González, and V.Cambiazo (2008).
Identification of woolliness response genes in peach fruit after post-harvest treatments.
  J Exp Bot, 59, 1973-1986.  
18066688 N.Krom, J.Recla, and W.Ramakrishna (2008).
Analysis of genes associated with retrotransposons in the rice genome.
  Genetica, 134, 297-310.  
17971035 N.Röckel, S.Wolf, B.Kost, T.Rausch, and S.Greiner (2008).
Elaborate spatial patterning of cell-wall PME and PMEI at the pollen tube tip involves PMEI endocytosis, and reflects the distribution of esterified and de-esterified pectins.
  Plant J, 53, 133-143.  
18327607 S.H.An, K.H.Sohn, H.W.Choi, I.S.Hwang, S.C.Lee, and B.K.Hwang (2008).
Pepper pectin methylesterase inhibitor protein CaPMEI1 is required for antifungal activity, basal disease resistance and abiotic stress tolerance.
  Planta, 228, 61-78.  
16699194 M.Hothorn, and K.Scheffzek (2006).
Multiple crystal forms of the cell-wall invertase inhibitor from tobacco support high conformational rigidity over a broad pH range.
  Acta Crystallogr D Biol Crystallogr, 62, 665-670.
PDB codes: 2cj4 2cj5 2cj6 2cj7 2cj8
16774842 N.Juge (2006).
Plant protein inhibitors of cell wall degrading enzymes.
  Trends Plant Sci, 11, 359-367.  
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 code is shown on the right.