PDBsum entry 1k30

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protein links
Transferase PDB id
Protein chain
363 a.a. *
Waters ×473
* Residue conservation analysis
PDB id:
Name: Transferase
Title: Crystal structure analysis of squash (cucurbita moschata) glycerol-3-phosphate (1)-acyltransferase
Structure: Glycerol-3-phosphate acyltransferase. Chain: a. Synonym: glycerol-3-phosphate (1)-acyltransferase, gpat. Engineered: yes
Source: Cucurbita moschata. Crookneck pumpkin. Organism_taxid: 3662. Gene: plsb. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
1.90Å     R-factor:   0.188     R-free:   0.224
Authors: A.P.Turnbull,J.B.Rafferty,S.E.Sedelnikova,A.R.Slabas, T.P.Schierer,J.T.Kroon,J.W.Simon,T.Fawcett,I.Nishida, N.Murata,D.W.Rice
Key ref:
A.P.Turnbull et al. (2001). Analysis of the structure, substrate specificity, and mechanism of squash glycerol-3-phosphate (1)-acyltransferase. Structure, 9, 347-353. PubMed id: 11377195 DOI: 10.1016/S0969-2126(01)00595-0
01-Oct-01     Release date:   31-Oct-01    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P10349  (PLSB_CUCMO) -  Glycerol-3-phosphate acyltransferase, chloroplastic
396 a.a.
363 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.  - Glycerol-3-phosphate 1-O-acyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate
+ sn-glycerol 3-phosphate
= CoA
+ 1-acyl-sn-glycerol 3-phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     plastid   3 terms 
  Biological process     metabolic process   5 terms 
  Biochemical function     transferase activity     3 terms  


DOI no: 10.1016/S0969-2126(01)00595-0 Structure 9:347-353 (2001)
PubMed id: 11377195  
Analysis of the structure, substrate specificity, and mechanism of squash glycerol-3-phosphate (1)-acyltransferase.
A.P.Turnbull, J.B.Rafferty, S.E.Sedelnikova, A.R.Slabas, T.P.Schierer, J.T.Kroon, J.W.Simon, T.Fawcett, I.Nishida, N.Murata, D.W.Rice.
BACKGROUND: Glycerol-3-phosphate (1)-acyltransferase(G3PAT) catalyzes the incorporation of an acyl group from either acyl-acyl carrier proteins (acylACPs) or acyl-CoAs into the sn-1 position of glycerol 3-phosphate to yield 1-acylglycerol-3-phosphate. G3PATs can either be selective, preferentially using the unsaturated fatty acid, oleate (C18:1), as the acyl donor, or nonselective, using either oleate or the saturated fatty acid, palmitate (C16:0), at comparable rates. The differential substrate specificity for saturated versus unsaturated fatty acids seen within this enzyme family has been implicated in the sensitivity of plants to chilling temperatures. RESULTS: The three-dimensional structure of recombinant G3PAT from squash chloroplast has been determined to 1.9 A resolution by X-ray crystallography using the technique of multiple isomorphous replacement and provides the first representative structure of an enzyme of this class. CONCLUSIONS: The tertiary structure of G3PAT comprises two domains, the larger of which, domain II, features an extensive cleft lined by hydrophobic residues and contains at one end a cluster of positively charged residues flanked by a H(X)(4)D motif, which is conserved amongst many glycerolipid acyltransferases. We predict that these hydrophobic and positively charged residues represent the binding sites for the fatty acyl substrate and the phosphate moiety of the glycerol 3-phosphate, respectively, and that the H(X)(4)D motif is a critical component of the enzyme's catalytic machinery.
  Selected figure(s)  
Figure 2.
Figure 2. Stereo Diagrams of Squash G3PAT(a) A schematic representation with the strands and helices labeled and colored red and green, respectively. The figure was prepared using MOLSCRIPT [26].(b) Ca trace with every tenth residue dotted and every twentieth residue numbered. The pattern of sequence conservation across members of the G3PAT family is also illustrated. Residues that are fully conserved across all five representative G3PAT sequences are colored green, residues that are fully conserved in chilling-resistant (arabidopsis, pea, and spinach) plants but differ in chilling-sensitive plants (squash and cucumber) are highlighted in red, and the remainder are highlighted in blue. The modeled positions of the glycerol 3-phosphate and fatty acyl substrate moieties are shown in atom colors (carbon, white; oxygen, red; and phosphate, pink) and cyan, respectively. The figure was prepared using MIDAS PLUS [27 and 28]

  The above figure is reprinted by permission from Cell Press: Structure (2001, 9, 347-353) copyright 2001.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21494142 M.Oberer, A.Boeszoermenyi, H.M.Nagy, and R.Zechner (2011).
Recent insights into the structure and function of comparative gene identification-58.
  Curr Opin Lipidol, 22, 149-158.  
19879895 J.Joyard, M.Ferro, C.Masselon, D.Seigneurin-Berny, D.Salvi, J.Garin, and N.Rolland (2010).
Chloroplast proteomics highlights the subcellular compartmentation of lipid metabolism.
  Prog Lipid Res, 49, 128-158.  
19336658 K.Takeuchi, and K.Reue (2009).
Biochemistry, physiology, and genetics of GPAT, AGPAT, and lipin enzymes in triglyceride synthesis.
  Am J Physiol Endocrinol Metab, 296, E1195-E1209.  
19903225 S.Q.Zhu, H.Zhao, R.Zhou, B.H.Ji, and X.Y.Dan (2009).
Substrate Selectivity of Glycerol-3-phosphate Acyl Transferase in Rice.
  J Integr Plant Biol, 51, 1040-1049.  
18369234 Y.M.Zhang, and C.O.Rock (2008).
Thematic review series: Glycerolipids. Acyltransferases in bacterial glycerophospholipid synthesis.
  J Lipid Res, 49, 1867-1874.  
16552061 K.P.Robertson, C.J.Smith, A.M.Gough, and E.R.Rocha (2006).
Characterization of Bacteroides fragilis hemolysins and regulation and synergistic interactions of HlyA and HlyB.
  Infect Immun, 74, 2304-2316.  
12944395 K.Johansson, J.M.Bourhis, V.Campanacci, C.Cambillau, B.Canard, and S.Longhi (2003).
Crystal structure of the measles virus phosphoprotein domain responsible for the induced folding of the C-terminal domain of the nucleoprotein.
  J Biol Chem, 278, 44567-44573.
PDB code: 1oks
  14498826 L.Bonham, D.W.Leung, T.White, D.Hollenback, P.Klein, J.Tulinsky, M.Coon, Vries, and J.W.Singer (2003).
Lysophosphatidic acid acyltransferase-beta: a novel target for induction of tumour cell apoptosis.
  Expert Opin Ther Targets, 7, 643-661.  
12205087 A.R.Slabas, J.T.Kroon, T.P.Scheirer, J.S.Gilroy, M.Hayman, D.W.Rice, A.P.Turnbull, J.B.Rafferty, T.Fawcett, and W.J.Simon (2002).
Squash glycerol-3-phosphate (1)-acyltransferase. Alteration of substrate selectivity and identification of arginine and lysine residues important in catalytic activity.
  J Biol Chem, 277, 43918-43923.  
12419229 V.Kumar, J.E.Carlson, K.A.Ohgi, T.A.Edwards, D.W.Rose, C.R.Escalante, M.G.Rosenfeld, and A.K.Aggarwal (2002).
Transcription corepressor CtBP is an NAD(+)-regulated dehydrogenase.
  Mol Cell, 10, 857-869.
PDB code: 1mx3
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.