1iim: Difference between revisions

Revision as of 12:16, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1iim.png

Template:STRUCTURE 1iim

thymidylyltransferase complexed with TTPthymidylyltransferase complexed with TTP

Template:ABSTRACT PUBMED 11373625

About this StructureAbout this Structure

1IIM is a Single protein structure of sequence from Salmonella enterica. Full crystallographic information is available from OCA.

ReferenceReference

Structure, mechanism and engineering of a nucleotidylyltransferase as a first step toward glycorandomization., Barton WA, Lesniak J, Biggins JB, Jeffrey PD, Jiang J, Rajashankar KR, Thorson JS, Nikolov DB, Nat Struct Biol. 2001 Jun;8(6):545-51. PMID:11373625

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OCA

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-'''thymidylyltransferase complexed with TTP'''
+===thymidylyltransferase complexed with TTP===
-==Overview==
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-Metabolite glycosylation is affected by three classes of enzymes: nucleotidylyltransferases, which activate sugars as nucleotide diphospho-derivatives, intermediate sugar-modifying enzymes and glycosyltransferases, which transfer the final derivatized activated sugars to aglycon substrates. One of the first crystal structures of an enzyme responsible for the first step in this cascade, alpha-D-glucopyranosyl phosphate thymidylyltransferase (Ep) from Salmonella, in complex with product (UDP-Glc) and substrate (dTTP) is reported at 2.0 A and 2.1 A resolution, respectively. These structures, in conjunction with the kinetic characterization of Ep, clarify the catalytic mechanism of this important enzyme class. Structure-based engineering of Ep produced modified enzymes capable of utilizing 'unnatural' sugar phosphates not accepted by wild type Ep. The demonstrated ability to alter nucleotidylyltransferase specificity by design is an integral component of in vitro glycosylation systems developed for the production of diverse glycorandomized libraries.
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 [[Category: Thorson, J S.]]
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