1iin: Difference between revisions

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-[[Image:1iin.jpg|left|200px]]<br /><applet load="1iin" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="1iin, resolution 2.10&Aring;" />
-'''thymidylyltransferase complexed with UDP-glucose'''<br />
-==Overview==
+==thymidylyltransferase complexed with UDP-glucose==
-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.
+<StructureSection load='1iin' size='340' side='right'caption='[[1iin]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1iin]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica Salmonella enterica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IIN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IIN FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UPG:URIDINE-5-DIPHOSPHATE-GLUCOSE'>UPG</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1iin FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iin OCA], [https://pdbe.org/1iin PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iin RCSB], [https://www.ebi.ac.uk/pdbsum/1iin PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iin ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/RMLA_SALTY RMLA_SALTY] Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. Is also able to convert non natural substrates such as a wide array of alpha-D-hexopyranosyl, deoxy-alpha-D-glucopyranosyl, aminodeoxy-alpha-D-hexopyranosyl and acetamidodeoxy-alpha-D-hexopyranosyl phosphates to their corresponding dTDP- and UDP-nucleotide sugars.<ref>PMID:8382158</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ii/1iin_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1iin ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-IIN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_enterica Salmonella enterica] with <scene name='pdbligand=UPG:'>UPG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glucose-1-phosphate_thymidylyltransferase Glucose-1-phosphate thymidylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.24 2.7.7.24] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IIN OCA].
+*[[Glucose-1-phosphate thymidylyltransferase 3D structures|Glucose-1-phosphate thymidylyltransferase 3D structures]]
+== References ==
-==Reference==
+<references/>
-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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11373625 11373625]
+__TOC__
-[[Category: Glucose-1-phosphate thymidylyltransferase]]
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Salmonella enterica]]
-[[Category: Single protein]]
+[[Category: Barton WA]]
-[[Category: Barton, W A.]]
+[[Category: Biggins JB]]
-[[Category: Biggins, J B.]]
+[[Category: Jeffrey PD]]
-[[Category: Jeffrey, P D.]]
+[[Category: Jiang J]]
-[[Category: Jiang, J.]]
+[[Category: Lesniak J]]
-[[Category: Lesniak, J.]]
+[[Category: Nikolov DB]]
-[[Category: Nikolov, D B.]]
+[[Category: Rajashankar KR]]
-[[Category: Rajashankar, K R.]]
+[[Category: Thorson JS]]
-[[Category: Thorson, J S.]]
-[[Category: UPG]]
-[[Category: transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:12:17 2008''