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1odu

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[[Image:1odu.png|left|200px]]
[[Image:1odu.png|left|200px]]
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{{STRUCTURE_1odu| PDB=1odu | SCENE= }}
{{STRUCTURE_1odu| PDB=1odu | SCENE= }}
===CRYSTAL STRUCTURE OF THERMOTOGA MARITIMA ALPHA-FUCOSIDASE IN COMPLEX WITH FUCOSE===
===CRYSTAL STRUCTURE OF THERMOTOGA MARITIMA ALPHA-FUCOSIDASE IN COMPLEX WITH FUCOSE===
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==Reference==
==Reference==
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<ref group="xtra">PMID:14715651</ref><ref group="xtra">PMID:12975375</ref><references group="xtra"/>
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<ref group="xtra">PMID:014715651</ref><ref group="xtra">PMID:012975375</ref><ref group="xtra">PMID:019875083</ref><references group="xtra"/>
[[Category: Alpha-L-fucosidase]]
[[Category: Alpha-L-fucosidase]]
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]

Revision as of 09:51, 16 January 2013

Template:STRUCTURE 1odu

CRYSTAL STRUCTURE OF THERMOTOGA MARITIMA ALPHA-FUCOSIDASE IN COMPLEX WITH FUCOSE

Template:ABSTRACT PUBMED 14715651

About this Structure

1odu is a 2 chain structure with sequence from Thermotoga maritima. Full crystallographic information is available from OCA.

Reference

  • Sulzenbacher G, Bignon C, Nishimura T, Tarling CA, Withers SG, Henrissat B, Bourne Y. Crystal structure of Thermotoga maritima alpha-L-fucosidase. Insights into the catalytic mechanism and the molecular basis for fucosidosis. J Biol Chem. 2004 Mar 26;279(13):13119-28. Epub 2004 Jan 8. PMID:14715651 doi:10.1074/jbc.M313783200
  • Tarling CA, He S, Sulzenbacher G, Bignon C, Bourne Y, Henrissat B, Withers SG. Identification of the catalytic nucleophile of the family 29 alpha-L-fucosidase from Thermotoga maritima through trapping of a covalent glycosyl-enzyme intermediate and mutagenesis. J Biol Chem. 2003 Nov 28;278(48):47394-9. Epub 2003 Sep 15. PMID:12975375 doi:http://dx.doi.org/10.1074/jbc.M306610200
  • Cobucci-Ponzano B, Conte F, Bedini E, Corsaro MM, Parrilli M, Sulzenbacher G, Lipski A, Dal Piaz F, Lepore L, Rossi M, Moracci M. beta-Glycosyl azides as substrates for alpha-glycosynthases: preparation of efficient alpha-L-fucosynthases. Chem Biol. 2009 Oct 30;16(10):1097-108. PMID:19875083 doi:10.1016/j.chembiol.2009.09.013

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