1iim

<table><tr><td colspan='2'>[[1iim]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_cholerae-suis"_smith_1894 "bacillus cholerae-suis" smith 1894]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IIM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IIM FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TTP:THYMIDINE-5-TRIPHOSPHATE'>TTP</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1iin|1iin]], [[1mp3|1mp3]], [[1mp4|1mp4]], [[1mp5|1mp5]]</div></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glucose-1-phosphate_thymidylyltransferase Glucose-1-phosphate thymidylyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.24 2.7.7.24] </span></td></tr>

[[https://www.uniprot.org/uniprot/Q9F7K6_SALCE Q9F7K6_SALCE]] Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis (By similarity).[RuleBase:RU003706]

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:11373625</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1iim" style="background-color:#fffaf0;"></div>

[[Category: Bacillus cholerae-suis smith 1894]]

[[Category: Glucose-1-phosphate thymidylyltransferase]]

[[Category: Barton, W A]]

[[Category: Biggins, J B]]

[[Category: Jeffrey, P D]]

[[Category: Jiang, J]]

[[Category: Lesniak, J]]

[[Category: Nikolov, D B]]

[[Category: Rajashankar, K R]]

[[Category: Thorson, J S]]

[[Category: Transferase]]