1kiz
From Proteopedia
(New page: 200px<br /><applet load="1kiz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kiz, resolution 2.60Å" /> '''D100E trichodiene sy...) |
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| - | [[Image:1kiz.jpg|left|200px]]<br /><applet load="1kiz" size=" | + | [[Image:1kiz.jpg|left|200px]]<br /><applet load="1kiz" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1kiz, resolution 2.60Å" /> | caption="1kiz, resolution 2.60Å" /> | ||
'''D100E trichodiene synthase complexed with pyrophosphate'''<br /> | '''D100E trichodiene synthase complexed with pyrophosphate'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The 2.4 A resolution X-ray crystal structure of D100E trichodiene synthase | + | The 2.4 A resolution X-ray crystal structure of D100E trichodiene synthase and the 2.6 A resolution structure of its complex with inorganic pyrophosphate are reported. The D100E amino acid substitution in the so-called "aspartate-rich" motif does not result in large changes to the overall structure of the enzyme. In the pyrophosphate complex, however, pyrophosphate coordinates two Mg(2+) ions at the mouth of the active site without causing large changes in the structure of the enzyme. This contrasts with pyrophosphate binding in the wild-type enzyme, where pyrophosphate coordinates three Mg(2+) ions and triggers a significant conformational change that closes the mouth of the active site and optimizes packing density in the enzyme-substrate complex. The attenuation of active site closure in D100E trichodiene synthase compromises enzyme-substrate packing density and confers additional spatial and conformational degrees of freedom on the substrate and carbocation intermediates, which in turn results in the formation of five alternate sesquiterpene products in addition to trichodiene. By extension, then, the diversity of terpene cyclases in biology may have evolved in part by amino acid substitutions that fine-tune structural changes dependent on metal-diphosphate complexation that govern the formation of the active site template and enzyme-substrate packing density. |
==About this Structure== | ==About this Structure== | ||
| - | 1KIZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Fusarium_sporotrichioides Fusarium sporotrichioides] with MG, POP and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Trichodiene_synthase Trichodiene synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.3.6 4.2.3.6] Full crystallographic information is available from [http:// | + | 1KIZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Fusarium_sporotrichioides Fusarium sporotrichioides] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=POP:'>POP</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Trichodiene_synthase Trichodiene synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.3.6 4.2.3.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KIZ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Trichodiene synthase]] | [[Category: Trichodiene synthase]] | ||
| - | [[Category: Cane, D | + | [[Category: Cane, D E.]] |
| - | [[Category: Christianson, D | + | [[Category: Christianson, D W.]] |
| - | [[Category: Rynkiewicz, M | + | [[Category: Rynkiewicz, M J.]] |
[[Category: EDO]] | [[Category: EDO]] | ||
[[Category: MG]] | [[Category: MG]] | ||
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[[Category: terpenoid synthase fold]] | [[Category: terpenoid synthase fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:34:41 2008'' |
Revision as of 11:34, 21 February 2008
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D100E trichodiene synthase complexed with pyrophosphate
Overview
The 2.4 A resolution X-ray crystal structure of D100E trichodiene synthase and the 2.6 A resolution structure of its complex with inorganic pyrophosphate are reported. The D100E amino acid substitution in the so-called "aspartate-rich" motif does not result in large changes to the overall structure of the enzyme. In the pyrophosphate complex, however, pyrophosphate coordinates two Mg(2+) ions at the mouth of the active site without causing large changes in the structure of the enzyme. This contrasts with pyrophosphate binding in the wild-type enzyme, where pyrophosphate coordinates three Mg(2+) ions and triggers a significant conformational change that closes the mouth of the active site and optimizes packing density in the enzyme-substrate complex. The attenuation of active site closure in D100E trichodiene synthase compromises enzyme-substrate packing density and confers additional spatial and conformational degrees of freedom on the substrate and carbocation intermediates, which in turn results in the formation of five alternate sesquiterpene products in addition to trichodiene. By extension, then, the diversity of terpene cyclases in biology may have evolved in part by amino acid substitutions that fine-tune structural changes dependent on metal-diphosphate complexation that govern the formation of the active site template and enzyme-substrate packing density.
About this Structure
1KIZ is a Single protein structure of sequence from Fusarium sporotrichioides with , and as ligands. Active as Trichodiene synthase, with EC number 4.2.3.6 Full crystallographic information is available from OCA.
Reference
X-ray crystal structures of D100E trichodiene synthase and its pyrophosphate complex reveal the basis for terpene product diversity., Rynkiewicz MJ, Cane DE, Christianson DW, Biochemistry. 2002 Feb 12;41(6):1732-41. PMID:11827517
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