3sxp: Difference between revisions
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<StructureSection load='3sxp' size='340' side='right' caption='[[3sxp]], [[Resolution|resolution]] 2.55Å' scene=''> | <StructureSection load='3sxp' size='340' side='right' caption='[[3sxp]], [[Resolution|resolution]] 2.55Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3sxp]] is a 5 chain structure | <table><tr><td colspan='2'>[[3sxp]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SXP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SXP FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1eq2|1eq2]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1eq2|1eq2]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/ADP-glyceromanno-heptose_6-epimerase ADP-glyceromanno-heptose 6-epimerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.3.20 5.1.3.20] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/ADP-glyceromanno-heptose_6-epimerase ADP-glyceromanno-heptose 6-epimerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.3.20 5.1.3.20] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3sxp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sxp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3sxp RCSB], [http://www.ebi.ac.uk/pdbsum/3sxp PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3sxp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sxp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3sxp RCSB], [http://www.ebi.ac.uk/pdbsum/3sxp PDBsum]</span></td></tr> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: ADP-glyceromanno-heptose 6-epimerase]] | [[Category: ADP-glyceromanno-heptose 6-epimerase]] | ||
[[Category: Cendron, L]] | |||
[[Category: Cendron, L | [[Category: Shaik, M M]] | ||
[[Category: Shaik, M M | [[Category: Zanotti, G]] | ||
[[Category: Zanotti, G | |||
[[Category: Epimerase]] | [[Category: Epimerase]] | ||
[[Category: Isomerase]] | [[Category: Isomerase]] | ||
[[Category: Nad binding]] | [[Category: Nad binding]] | ||
[[Category: Rossmann fold]] | [[Category: Rossmann fold]] | ||
Revision as of 10:30, 12 November 2014
Crystal Structure of Helicobacter pylori ADP-L-glycero-D-manno-heptose-6-epimerase (rfaD, HP0859)Crystal Structure of Helicobacter pylori ADP-L-glycero-D-manno-heptose-6-epimerase (rfaD, HP0859)
Structural highlights
Publication Abstract from PubMedHelicobacter pylori, the human pathogen that affects about half of the world population and that is responsible for gastritis, gastric ulcer and adenocarcinoma and MALT lymphoma, owes much of the integrity of its outer membrane on lipopolysaccharides (LPSs). Together with their essential structural role, LPSs contribute to the bacterial adherence properties, as well as they are well characterized for the capability to modulate the immuno-response. In H. pylori the core oligosaccharide, one of the three main domains of LPSs, shows a peculiar structure in the branching organization of the repeating units, which displayed further variability when different strains have been compared. We present here the crystal structure of ADP-L-glycero-D-manno-heptose-6-epimerase (HP0859, rfaD), the last enzyme in the pathway that produces L-glycero-D-manno-heptose starting from sedoheptulose-7-phosphate, a crucial compound in the synthesis of the core oligosaccharide. In a recent study, a HP0859 knockout mutant has been characterized, demonstrating a severe loss of lipopolysaccharide structure and a significant reduction of adhesion levels in an infection model to AGS cells, if compared with the wild type strain, in good agreement with its enzymatic role. The crystal structure reveals that the enzyme is a homo-pentamer, and NAD is bound as a cofactor in a highly conserved pocket. The substrate-binding site of the enzyme is very similar to that of its orthologue in Escherichia coli, suggesting also a similar catalytic mechanism. The crystal structure of ADP-L-glycero-D-manno-heptose-6-epimerase (HP0859) from Helicobacter pylori.,Shaik MM, Zanotti G, Cendron L Biochim Biophys Acta. 2011 Dec;1814(12):1641-7. Epub 2011 Sep 25. PMID:21979583[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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