1iuq: Difference between revisions

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[[Image:1iuq.~~gif~~|left|200px]]

[[Image:1iuq.png|left|200px]]

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

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

~~==Overview==~~

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~~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~~.

The line below this paragraph, {{ABSTRACT_PUBMED_14684887}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 14684887 is the PubMed ID number.

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==About this Structure==

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[[Category: Four helix bundle]]

[[Category: Open twisted alpha/beta]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 20~~:26:22 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 14:02:09 2008''

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-[[Image:1iuq.gif|left|200px]]
+{{Seed}}
+[[Image:1iuq.png|left|200px]]
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 {{STRUCTURE_1iuq|  PDB=1iuq  |  SCENE=  }}
-'''The 1.55 A Crystal Structure of Glycerol-3-Phosphate Acyltransferase'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_14684887}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14684887 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_14684887}}
 ==About this Structure==
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 [[Category: Four helix bundle]]
 [[Category: Open twisted alpha/beta]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 20:26:22 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 14:02:09 2008''