1K30

Crystal Structure Analysis of Squash (Cucurbita moschata) glycerol-3-phosphate (1)-acyltransferase

Summary for 1K30

• Entry DOI: 10.2210/pdb1k30/pdb
• Descriptor: glycerol-3-phosphate acyltransferase (2 entities in total)
• Functional Keywords: four-helix bundle, transferase
• Biological source: Cucurbita moschata (crookneck pumpkin)
• Cellular location: Plastid, chloroplast stroma: P10349
• Total number of polymer chains: 1
• Total formula weight: 40968.56

Authors

Turnbull, A.P.,Rafferty, J.B.,Sedelnikova, S.E.,Slabas, A.R.,Schierer, T.P.,Kroon, J.T.,Simon, J.W.,Fawcett, T.,Nishida, I.,Murata, N.,Rice, D.W. (deposition date: 2001-10-01, release date: 2001-10-31, Last modification date: 2024-02-07)

Primary citation

Turnbull, A.P.,Rafferty, J.B.,Sedelnikova, S.E.,Slabas, A.R.,Schierer, T.P.,Kroon, J.T.,Simon, J.W.,Fawcett, T.,Nishida, I.,Murata, N.,Rice, D.W.
Analysis of the structure, substrate specificity, and mechanism of squash glycerol-3-phosphate (1)-acyltransferase.
Structure, 9:347-353, 2001

PubMed Abstract: 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.

PubMed: 11377195
DOI: 10.1016/S0969-2126(01)00595-0

Experimental method

X-RAY DIFFRACTION (1.9 Å)