View source for 2h1h


==E. coli heptosyltransferase WaaC with ADP-2-deoxy-2-fluoro heptose==
<StructureSection load='2h1h' size='340' side='right'caption='[[2h1h]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2h1h]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_RS218 Escherichia coli RS218]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H1H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H1H 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]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AFH:ADENOSINE-5-DIPHOSPHATE-2-DEOXY-2-FLUORO+HEPTOSE'>AFH</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=2h1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h1h OCA], [https://pdbe.org/2h1h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h1h RCSB], [https://www.ebi.ac.uk/pdbsum/2h1h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h1h ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RFAC_ECOLI RFAC_ECOLI] Heptose transfer to the lipopolysaccharide core. It transfers the innermost heptose to [4'-P](3-deoxy-D-manno-octulosonic acid)2-IVA.
== 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/h1/2h1h_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=2h1h ConSurf].
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== 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>
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<div class="pdbe-citations 2h1h" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli RS218]]
[[Category: Large Structures]]
[[Category: Dohi H]]
[[Category: Ducruix A]]
[[Category: Durand L]]
[[Category: Escaich S]]
[[Category: Grizot S]]
[[Category: Moreau F]]
[[Category: Salem M]]
[[Category: Vincent S]]
[[Category: Vongsouthi V]]