1IUQ

The 1.55 A Crystal Structure of Glycerol-3-Phosphate Acyltransferase

Summary for 1IUQ

• Entry DOI: 10.2210/pdb1iuq/pdb
• Descriptor: Glycerol-3-Phosphate Acyltransferase, SULFATE ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: open twisted alpha/beta, 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: 42198.50

Authors

Tamada, T.,Feese, M.D.,Kato, Y.,Kuroki, R. (deposition date: 2002-03-06, release date: 2003-10-07, Last modification date: 2024-10-09)

Primary citation

Tamada, T.,Feese, M.D.,Ferri, S.R.,Kato, Y.,Yajima, R.,Toguri, T.,Kuroki, R.
Substrate recognition and selectivity of plant glycerol-3-phosphate acyltransferases (GPATs) from Cucurbita moscata and Spinacea oleracea.
Acta Crystallogr.,Sect.D, 60:13-21, 2004

PubMed 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.

PubMed: 14684887
DOI: 10.1107/S0907444903020778

Experimental method

X-RAY DIFFRACTION (1.55 Å)