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PDBsum entry 1iuq

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protein ligands links
Transferase PDB id
1iuq
Jmol
Contents
Protein chain
357 a.a. *
Ligands
SO4 ×5
GOL ×6
Waters ×390
* Residue conservation analysis
PDB id:
1iuq
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.
Resolution:
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
Date:
06-Mar-02     Release date:   07-Oct-03    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P10349  (PLSB_CUCMO) -  Glycerol-3-phosphate acyltransferase, chloroplastic
Seq:
Struc:
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.2.3.1.15  - Glycerol-3-phosphate 1-O-acyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate
Acyl-CoA
+
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  

 

 
    reference    
 
 
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.
 
  ABSTRACT  
 
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
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.