3g5i

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'''Unreleased structure'''
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{{Seed}}
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[[Image:3g5i.jpg|left|200px]]
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The entry 3g5i is ON HOLD until Paper Publication
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{{STRUCTURE_3g5i| PDB=3g5i | SCENE= }}
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Authors: Garau, G., Muzzolini, L., Tornaghi, P., Degano, M.
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===Crystal Structure of the E.coli RihA pyrimidine nucleosidase bound to a iminoribitol-based inhibitor===
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Description: Crystal Structure of the E.coli RihA pyrimidine nucleosidase bound to a iminoribitol-based inhibitor
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 22 10:24:00 2009''
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==About this Structure==
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3G5I is a 4 chains structure with sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G5I OCA].
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==Reference==
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<ref group="xtra">PMID:16411753</ref><ref group="xtra">PMID:15130467</ref><references group="xtra"/>
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[[Category: Escherichia coli]]
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[[Category: Ribosylpyrimidine nucleosidase]]
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[[Category: Degano, M.]]
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[[Category: Garau, G.]]
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[[Category: Muzzolini, L.]]
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[[Category: Tornaghi, P.]]
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[[Category: Glycosidase]]
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[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 10 17:52:56 2010''

Revision as of 15:52, 10 February 2010

Image:3g5i.jpg

Template:STRUCTURE 3g5i

Crystal Structure of the E.coli RihA pyrimidine nucleosidase bound to a iminoribitol-based inhibitor

About this Structure

3G5I is a 4 chains structure with sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

  • Muzzolini L, Versees W, Tornaghi P, Van Holsbeke E, Steyaert J, Degano M. New insights into the mechanism of nucleoside hydrolases from the crystal structure of the Escherichia coli YbeK protein bound to the reaction product. Biochemistry. 2006 Jan 24;45(3):773-82. PMID:16411753 doi:10.1021/bi0511991
  • Giabbai B, Degano M. Crystal structure to 1.7 a of the Escherichia coli pyrimidine nucleoside hydrolase YeiK, a novel candidate for cancer gene therapy. Structure. 2004 May;12(5):739-49. PMID:15130467 doi:http://dx.doi.org/10.1016/j.str.2004.03.018

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