2gt1: Difference between revisions

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 <StructureSection load='2gt1' size='340' side='right'caption='[[2gt1]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2gt1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecout Ecout]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GT1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GT1 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2gt1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_UTI89 Escherichia coli UTI89]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GT1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GT1 FirstGlance]. <br>
-</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=2gt1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gt1 OCA], [https://pdbe.org/2gt1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gt1 RCSB], [https://www.ebi.ac.uk/pdbsum/2gt1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gt1 ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</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=2gt1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gt1 OCA], [https://pdbe.org/2gt1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gt1 RCSB], [https://www.ebi.ac.uk/pdbsum/2gt1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gt1 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q1R4X0_ECOUT Q1R4X0_ECOUT]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 16: / Line 19: @@
 </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=2gt1 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Lipopolysaccharides constitute the outer leaflet of the outer membrane of Gram-negative bacteria and are therefore essential for cell growth and viability. The heptosyltransferase WaaC is a glycosyltransferase (GT) involved in the synthesis of the inner core region of LPS. It catalyzes the addition of the first L-glycero-D-manno-heptose (heptose) molecule to one 3-deoxy-D-manno-oct-2-ulosonic acid (Kdo) residue of the Kdo2-lipid A molecule. Heptose is an essential component of the LPS core domain; its absence results in a truncated lipopolysaccharide associated with the deep-rough phenotype causing a greater susceptibility to antibiotic and an attenuated virulence for pathogenic Gram-negative bacteria. Thus, WaaC represents a promising target in antibacterial drug design. Here, we report the structure of WaaC from the Escherichia coli pathogenic strain RS218 alone at 1.9 A resolution, and in complex with either ADP or the non-cleavable analog ADP-2-deoxy-2-fluoro-heptose of the sugar donor at 2.4 A resolution. WaaC adopts the GT-B fold in two domains, characteristic of one glycosyltransferase structural superfamily. The comparison of the three different structures shows that WaaC does not undergo a domain rotation, characteristic of the GT-B family, upon substrate binding, but allows the substrate analog and the reaction product to adopt remarkably distinct conformations inside the active site. In addition, both binary complexes offer a close view of the donor subsite and, together with results from site-directed mutagenesis studies, provide evidence for a model of the catalytic mechanism.
-Structure of the Escherichia coli heptosyltransferase WaaC: binary complexes with ADP and ADP-2-deoxy-2-fluoro heptose.,Grizot S, Salem M, Vongsouthi V, Durand L, Moreau F, Dohi H, Vincent S, Escaich S, Ducruix A J Mol Biol. 2006 Oct 20;363(2):383-94. Epub 2006 Jul 29. PMID:16963083<ref>PMID:16963083</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 2gt1" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Ecout]]
+[[Category: Escherichia coli UTI89]]
 [[Category: Large Structures]]
-[[Category: Dohi, H]]
+[[Category: Dohi H]]
-[[Category: Ducruix, A]]
+[[Category: Ducruix A]]
-[[Category: Durand, L]]
+[[Category: Durand L]]
-[[Category: Escaich, S]]
+[[Category: Escaich S]]
-[[Category: Grizot, S]]
+[[Category: Grizot S]]
-[[Category: Moreau, F]]
+[[Category: Moreau F]]
-[[Category: Salem, M]]
+[[Category: Salem M]]
-[[Category: Vincent, S]]
+[[Category: Vincent S]]
-[[Category: Vongsouthi, V]]
+[[Category: Vongsouthi V]]
-[[Category: Gt-b fold]]
-[[Category: Transferase]]