1k30
From Proteopedia
(New page: 200px<br /><applet load="1k30" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k30, resolution 1.9Å" /> '''Crystal Structure Ana...) |
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| - | [[Image:1k30.gif|left|200px]]<br /><applet load="1k30" size=" | + | [[Image:1k30.gif|left|200px]]<br /><applet load="1k30" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1k30, resolution 1.9Å" /> | caption="1k30, resolution 1.9Å" /> | ||
'''Crystal Structure Analysis of Squash (Cucurbita moschata) glycerol-3-phosphate (1)-acyltransferase'''<br /> | '''Crystal Structure Analysis of Squash (Cucurbita moschata) glycerol-3-phosphate (1)-acyltransferase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | BACKGROUND: Glycerol-3-phosphate (1)-acyltransferase(G3PAT) catalyzes the | + | BACKGROUND: Glycerol-3-phosphate (1)-acyltransferase(G3PAT) catalyzes the incorporation of an acyl group from either acyl-acyl carrier proteins (acylACPs) or acyl-CoAs into the sn-1 position of glycerol 3-phosphate to yield 1-acylglycerol-3-phosphate. G3PATs can either be selective, preferentially using the unsaturated fatty acid, oleate (C18:1), as the acyl donor, or nonselective, using either oleate or the saturated fatty acid, palmitate (C16:0), at comparable rates. The differential substrate specificity for saturated versus unsaturated fatty acids seen within this enzyme family has been implicated in the sensitivity of plants to chilling temperatures. RESULTS: The three-dimensional structure of recombinant G3PAT from squash chloroplast has been determined to 1.9 A resolution by X-ray crystallography using the technique of multiple isomorphous replacement and provides the first representative structure of an enzyme of this class. CONCLUSIONS: The tertiary structure of G3PAT comprises two domains, the larger of which, domain II, features an extensive cleft lined by hydrophobic residues and contains at one end a cluster of positively charged residues flanked by a H(X)(4)D motif, which is conserved amongst many glycerolipid acyltransferases. We predict that these hydrophobic and positively charged residues represent the binding sites for the fatty acyl substrate and the phosphate moiety of the glycerol 3-phosphate, respectively, and that the H(X)(4)D motif is a critical component of the enzyme's catalytic machinery. |
==About this Structure== | ==About this Structure== | ||
| - | 1K30 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cucurbita_moschata Cucurbita moschata]. 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:// | + | 1K30 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cucurbita_moschata Cucurbita moschata]. 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=1K30 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Fawcett, T.]] | [[Category: Fawcett, T.]] | ||
| - | [[Category: Kroon, J | + | [[Category: Kroon, J T.]] |
[[Category: Murata, N.]] | [[Category: Murata, N.]] | ||
[[Category: Nishida, I.]] | [[Category: Nishida, I.]] | ||
| - | [[Category: Rafferty, J | + | [[Category: Rafferty, J B.]] |
| - | [[Category: Rice, D | + | [[Category: Rice, D W.]] |
| - | [[Category: Schierer, T | + | [[Category: Schierer, T P.]] |
| - | [[Category: Sedelnikova, S | + | [[Category: Sedelnikova, S E.]] |
| - | [[Category: Simon, J | + | [[Category: Simon, J W.]] |
| - | [[Category: Slabas, A | + | [[Category: Slabas, A R.]] |
| - | [[Category: Turnbull, A | + | [[Category: Turnbull, A P.]] |
[[Category: four-helix bundle]] | [[Category: four-helix bundle]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:29:31 2008'' |
Revision as of 11:29, 21 February 2008
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Crystal Structure Analysis of Squash (Cucurbita moschata) glycerol-3-phosphate (1)-acyltransferase
Overview
BACKGROUND: Glycerol-3-phosphate (1)-acyltransferase(G3PAT) catalyzes the incorporation of an acyl group from either acyl-acyl carrier proteins (acylACPs) or acyl-CoAs into the sn-1 position of glycerol 3-phosphate to yield 1-acylglycerol-3-phosphate. G3PATs can either be selective, preferentially using the unsaturated fatty acid, oleate (C18:1), as the acyl donor, or nonselective, using either oleate or the saturated fatty acid, palmitate (C16:0), at comparable rates. The differential substrate specificity for saturated versus unsaturated fatty acids seen within this enzyme family has been implicated in the sensitivity of plants to chilling temperatures. RESULTS: The three-dimensional structure of recombinant G3PAT from squash chloroplast has been determined to 1.9 A resolution by X-ray crystallography using the technique of multiple isomorphous replacement and provides the first representative structure of an enzyme of this class. CONCLUSIONS: The tertiary structure of G3PAT comprises two domains, the larger of which, domain II, features an extensive cleft lined by hydrophobic residues and contains at one end a cluster of positively charged residues flanked by a H(X)(4)D motif, which is conserved amongst many glycerolipid acyltransferases. We predict that these hydrophobic and positively charged residues represent the binding sites for the fatty acyl substrate and the phosphate moiety of the glycerol 3-phosphate, respectively, and that the H(X)(4)D motif is a critical component of the enzyme's catalytic machinery.
About this Structure
1K30 is a Single protein structure of sequence from Cucurbita moschata. Active as Glycerol-3-phosphate O-acyltransferase, with EC number 2.3.1.15 Full crystallographic information is available from OCA.
Reference
Analysis of the structure, substrate specificity, and mechanism of squash glycerol-3-phosphate (1)-acyltransferase., Turnbull AP, Rafferty JB, Sedelnikova SE, Slabas AR, Schierer TP, Kroon JT, Simon JW, Fawcett T, Nishida I, Murata N, Rice DW, Structure. 2001 May 9;9(5):347-53. PMID:11377195
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