PDBsum entry 1iuq

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protein ligands links
Transferase PDB id
Protein chain
357 a.a. *
SO4 ×5
GOL ×6
Waters ×390
* Residue conservation analysis
PDB id:
Name: Transferase
Title: The 1.55 a crystal structure of glycerol-3-phosphate acyltra
Structure: Glycerol-3-phosphate acyltransferase. Chain: a. Engineered: yes
Source: Cucurbita moschata. Crookneck pumpkin. Organism_taxid: 3662. Expressed in: escherichia coli. Expression_system_taxid: 562.
1.55Å     R-factor:   0.202     R-free:   0.219
Authors: T.Tamada,M.D.Feese,Y.Kato,R.Kuroki
Key ref:
T.Tamada et al. (2004). Substrate recognition and selectivity of plant glycerol-3-phosphate acyltransferases (GPATs) from Cucurbita moscata and Spinacea oleracea. Acta Crystallogr D Biol Crystallogr, 60, 13-21. PubMed id: 14684887
06-Mar-02     Release date:   07-Oct-03    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P10349  (PLSB_CUCMO) -  Glycerol-3-phosphate acyltransferase, chloroplastic
396 a.a.
357 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 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
Bound ligand (Het Group name = GOL)
matches with 60.00% similarity
= 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  


Acta Crystallogr D Biol Crystallogr 60:13-21 (2004)
PubMed id: 14684887  
Substrate recognition and selectivity of plant glycerol-3-phosphate acyltransferases (GPATs) from Cucurbita moscata and Spinacea oleracea.
T.Tamada, M.D.Feese, S.R.Ferri, Y.Kato, R.Yajima, T.Toguri, R.Kuroki.
Stromal glycerol-3-phosphate acyltransferases (GPAT) are responsible for the selective incorporation of saturated and unsaturated fatty-acyl chains into chloroplast membranes, which is an important determinant of a plant's ability to tolerate chilling temperatures. The molecular mechanisms of plant chilling tolerance were elucidated by creating chimeric GPATs between squash (Cucurbita moscata, chilling-sensitive) and spinach (Spinacea oleracea, chilling-tolerant) and the results were interpreted using structural information on squash GPAT determined by X-ray crystallography at 1.55 A resolution. Enzymatic analysis of the chimeric GPATs showed that the chimeric GPATs containing the spinach region from residues 128 to 187 prefer the 18:1 unsaturated fatty acid rather than 16:0 saturated fatty acid. Structure analysis suggests that the size and character of the cavity that is formed from this region determines the specific recognition of acyl chains.

Literature references that cite this PDB file's key reference

  PubMed id Reference
23242369 H.Li, Z.Peng, X.Yang, W.Wang, J.Fu, J.Wang, Y.Han, Y.Chai, T.Guo, N.Yang, J.Liu, M.L.Warburton, Y.Cheng, X.Hao, P.Zhang, J.Zhao, Y.Liu, G.Wang, J.Li, and J.Yan (2012).
Genome-wide association study dissects the genetic architecture of oil biosynthesis in maize kernels.
  Nat Genet, 45, 43-50.  
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.  
16492764 T.Tamada, E.Honjo, Y.Maeda, T.Okamoto, M.Ishibashi, M.Tokunaga, and R.Kuroki (2006).
Homodimeric cross-over structure of the human granulocyte colony-stimulating factor (GCSF) receptor signaling complex.
  Proc Natl Acad Sci U S A, 103, 3135-3140.
PDB code: 2d9q
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