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1nio

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(New page: 200px<br /><applet load="1nio" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nio, resolution 2.00&Aring;" /> '''Crystal structure of...)
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[[Image:1nio.gif|left|200px]]<br /><applet load="1nio" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1nio.gif|left|200px]]<br /><applet load="1nio" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1nio, resolution 2.00&Aring;" />
caption="1nio, resolution 2.00&Aring;" />
'''Crystal structure of beta-luffin, a ribosome inactivating protein at 2.0A resolution'''<br />
'''Crystal structure of beta-luffin, a ribosome inactivating protein at 2.0A resolution'''<br />
==Overview==
==Overview==
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The crystal structure of beta-luffin at 2.0 A resolution was solved by the, molecular-replacement method using polyalanyl trichosanthin as the search, model. The structure was refined with CNS1.1, giving R(work) = 0.162 and, R(free) = 0.204. The r.m.s.d.s of the bond lengths and bond angles are, 0.008 A and 1.3 degrees, respectively. The overall structure is similar to, those of other type I RIPs. Three N-acetylglucosamine (Nag) molecules are, linked to residues Asn2, Asn78 and Asn85 of the protein.
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The crystal structure of beta-luffin at 2.0 A resolution was solved by the molecular-replacement method using polyalanyl trichosanthin as the search model. The structure was refined with CNS1.1, giving R(work) = 0.162 and R(free) = 0.204. The r.m.s.d.s of the bond lengths and bond angles are 0.008 A and 1.3 degrees, respectively. The overall structure is similar to those of other type I RIPs. Three N-acetylglucosamine (Nag) molecules are linked to residues Asn2, Asn78 and Asn85 of the protein.
==About this Structure==
==About this Structure==
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1NIO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Luffa_aegyptiaca Luffa aegyptiaca] with NAG 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NIO OCA].
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1NIO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Luffa_aegyptiaca Luffa aegyptiaca] with <scene name='pdbligand=NAG:'>NAG</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=1NIO OCA].
==Reference==
==Reference==
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[[Category: ribosome inactivating protein(rip)]]
[[Category: ribosome inactivating protein(rip)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:17:52 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:06:34 2008''

Revision as of 12:06, 21 February 2008


1nio, resolution 2.00Å

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Crystal structure of beta-luffin, a ribosome inactivating protein at 2.0A resolution

Overview

The crystal structure of beta-luffin at 2.0 A resolution was solved by the molecular-replacement method using polyalanyl trichosanthin as the search model. The structure was refined with CNS1.1, giving R(work) = 0.162 and R(free) = 0.204. The r.m.s.d.s of the bond lengths and bond angles are 0.008 A and 1.3 degrees, respectively. The overall structure is similar to those of other type I RIPs. Three N-acetylglucosamine (Nag) molecules are linked to residues Asn2, Asn78 and Asn85 of the protein.

About this Structure

1NIO is a Single protein structure of sequence from Luffa aegyptiaca 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 beta-luffin, a ribosome-inactivating protein, at 2.0 A resolution., Ma QJ, Li JH, Li HG, Wu S, Dong YC, Acta Crystallogr D Biol Crystallogr. 2003 Aug;59(Pt 8):1366-70. Epub 2003, Jul 23. PMID:12876337

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