1IUQ: The 1.55 A Crystal Structure Of Glycerol-3-phosphate Acyltransferase

Citation:
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.
PDB ID: 1IUQDownload
MMDB ID: 24581
PDB Deposition Date: 2002/3/6
Updated in MMDB: 2007/11
Experimental Method:
x-ray diffraction
Resolution: 1.55  Å
Source Organism:
Similar Structures:
Biological Unit for 1IUQ: monomeric; determined by author
Molecular Components in 1IUQ
Label Count Molecule
Protein (1 molecule)
1
Glycerol-3-phosphate Acyltransferase
Molecule annotation
Chemicals (11 molecules)
1
5
2
6
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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