1iuq

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(New page: 200px<br /><applet load="1iuq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iuq, resolution 1.550&Aring;" /> '''The 1.55 A Crystal ...)
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[[Image:1iuq.gif|left|200px]]<br /><applet load="1iuq" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1iuq.gif|left|200px]]<br /><applet load="1iuq" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1iuq, resolution 1.550&Aring;" />
caption="1iuq, resolution 1.550&Aring;" />
'''The 1.55 A Crystal Structure of Glycerol-3-Phosphate Acyltransferase'''<br />
'''The 1.55 A Crystal Structure of Glycerol-3-Phosphate Acyltransferase'''<br />
==Overview==
==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.
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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.
==About this Structure==
==About this Structure==
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1IUQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cucurbita_moschata Cucurbita moschata] with SO4 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glycerol-3-phosphate_O-acyltransferase Glycerol-3-phosphate O-acyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.15 2.3.1.15] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IUQ OCA].
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1IUQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cucurbita_moschata Cucurbita moschata] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glycerol-3-phosphate_O-acyltransferase Glycerol-3-phosphate O-acyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.15 2.3.1.15] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IUQ OCA].
==Reference==
==Reference==
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[[Category: Glycerol-3-phosphate O-acyltransferase]]
[[Category: Glycerol-3-phosphate O-acyltransferase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Feese, M.D.]]
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[[Category: Feese, M D.]]
[[Category: Kato, Y.]]
[[Category: Kato, Y.]]
[[Category: Kuroki, R.]]
[[Category: Kuroki, R.]]
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[[Category: open twisted alpha/beta]]
[[Category: open twisted alpha/beta]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:40:48 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:15:49 2008''

Revision as of 11:15, 21 February 2008


1iuq, resolution 1.550Å

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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 with and as ligands. Active as Glycerol-3-phosphate O-acyltransferase, with EC number 2.3.1.15 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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