1iuq
From Proteopedia
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| , resolution 1.550Å | |||||||
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| Ligands: | and | ||||||
| Activity: | Glycerol-3-phosphate O-acyltransferase, with EC number 2.3.1.15 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The 1.55 A Crystal Structure of Glycerol-3-Phosphate Acyltransferase
Overview
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.
About this Structure
1IUQ is a Single protein structure of sequence from Cucurbita moschata. Full crystallographic information is available from OCA.
Reference
Substrate recognition and selectivity of plant glycerol-3-phosphate acyltransferases (GPATs) from Cucurbita moscata and Spinacea oleracea., Tamada T, Feese MD, Ferri SR, Kato Y, Yajima R, Toguri T, Kuroki R, Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):13-21. Epub 2003, Dec 18. PMID:14684887
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