1tcs
From Proteopedia
(New page: 200px<br /><applet load="1tcs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tcs, resolution 1.7Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1tcs.jpg|left|200px]]<br /><applet load="1tcs" size=" | + | [[Image:1tcs.jpg|left|200px]]<br /><applet load="1tcs" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1tcs, resolution 1.7Å" /> | caption="1tcs, resolution 1.7Å" /> | ||
'''CRYSTAL STRUCTURE OF TRICHOSANTHIN-NADPH COMPLEX AT 1.7 ANGSTROMS RESOLUTION REVEALS ACTIVE-SITE ARCHITECTURE'''<br /> | '''CRYSTAL STRUCTURE OF TRICHOSANTHIN-NADPH COMPLEX AT 1.7 ANGSTROMS RESOLUTION REVEALS ACTIVE-SITE ARCHITECTURE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We describe here the crystal structure of the trichosanthin-NADPH complex | + | We describe here the crystal structure of the trichosanthin-NADPH complex determined at a resolution of 1.7 A. The adenine base stacks between Tyr 70 and Tyr 111. Arg 163, Glu 160 and Tyr 70 form hydrogen bonds to N(3), O(3') and, through a water molecule, to N(9) of adenosine, respectively. This is the first high resolution structure of a complex between a ribosome-inactivating protein and a substrate analogue, in which the electron density of the N-glycosidic bond is well defined and the preassociated water, thought to be responsible for hydrolyzing the N-C bond, is also explicitly elucidated. |
==About this Structure== | ==About this Structure== | ||
| - | 1TCS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Trichosanthes_kirilowii Trichosanthes kirilowii] with NDP as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/rRNA_N-glycosylase rRNA N-glycosylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.22 3.2.2.22] Full crystallographic information is available from [http:// | + | 1TCS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Trichosanthes_kirilowii Trichosanthes kirilowii] with <scene name='pdbligand=NDP:'>NDP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/rRNA_N-glycosylase rRNA N-glycosylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.22 3.2.2.22] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TCS OCA]. |
==Reference== | ==Reference== | ||
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[[Category: rRNA N-glycosylase]] | [[Category: rRNA N-glycosylase]] | ||
[[Category: Wang, Y.]] | [[Category: Wang, Y.]] | ||
| - | [[Category: Xia, Z | + | [[Category: Xia, Z X.]] |
| - | [[Category: Xiong, J | + | [[Category: Xiong, J P.]] |
[[Category: NDP]] | [[Category: NDP]] | ||
[[Category: toxin]] | [[Category: toxin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:12:09 2008'' |
Revision as of 13:12, 21 February 2008
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CRYSTAL STRUCTURE OF TRICHOSANTHIN-NADPH COMPLEX AT 1.7 ANGSTROMS RESOLUTION REVEALS ACTIVE-SITE ARCHITECTURE
Overview
We describe here the crystal structure of the trichosanthin-NADPH complex determined at a resolution of 1.7 A. The adenine base stacks between Tyr 70 and Tyr 111. Arg 163, Glu 160 and Tyr 70 form hydrogen bonds to N(3), O(3') and, through a water molecule, to N(9) of adenosine, respectively. This is the first high resolution structure of a complex between a ribosome-inactivating protein and a substrate analogue, in which the electron density of the N-glycosidic bond is well defined and the preassociated water, thought to be responsible for hydrolyzing the N-C bond, is also explicitly elucidated.
About this Structure
1TCS is a Single protein structure of sequence from Trichosanthes kirilowii with as ligand. Active as rRNA N-glycosylase, with EC number 3.2.2.22 Full crystallographic information is available from OCA.
Reference
Crystal structure of trichosanthin-NADPH complex at 1.7 A resolution reveals active-site architecture., Xiong JP, Xia ZX, Wang Y, Nat Struct Biol. 1994 Oct;1(10):695-700. PMID:7634073
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