4e8y

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Current revision (14:55, 14 March 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4e8y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_cenocepacia_J2315 Burkholderia cenocepacia J2315]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E8Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E8Y FirstGlance]. <br>
<table><tr><td colspan='2'>[[4e8y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_cenocepacia_J2315 Burkholderia cenocepacia J2315]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E8Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E8Y FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IHA:{[2-({[5-(2,6-DIMETHOXYPHENYL)-1,2,4-TRIAZIN-3-YL]AMINO}METHYL)-1,3-BENZOTHIAZOL-5-YL]OXY}ACETIC+ACID'>IHA</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=M7B:7-O-PHOSPHONO-D-GLYCERO-BETA-D-MANNO-HEPTOPYRANOSE'>M7B</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IHA:{[2-({[5-(2,6-DIMETHOXYPHENYL)-1,2,4-TRIAZIN-3-YL]AMINO}METHYL)-1,3-BENZOTHIAZOL-5-YL]OXY}ACETIC+ACID'>IHA</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=M7B:7-O-PHOSPHONO-D-GLYCERO-BETA-D-MANNO-HEPTOPYRANOSE'>M7B</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=4e8y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e8y OCA], [https://pdbe.org/4e8y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e8y RCSB], [https://www.ebi.ac.uk/pdbsum/4e8y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e8y ProSAT]</span></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=4e8y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e8y OCA], [https://pdbe.org/4e8y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e8y RCSB], [https://www.ebi.ac.uk/pdbsum/4e8y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e8y ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/B4EB35_BURCJ B4EB35_BURCJ]]
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[https://www.uniprot.org/uniprot/B4EB35_BURCJ B4EB35_BURCJ]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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As an essential constituent of the outer membrane of Gram-negative bacteria, lipopolysaccharide contributes significantly to virulence and antibiotic resistance. The lipopolysaccharide biosynthetic pathway therefore serves as a promising therapeutic target for antivirulence drugs and antibiotic adjuvants. Here we report the structural-functional studies of d-glycero-beta-d-manno-heptose 7-phosphate kinase (HldA), an absolutely conserved enzyme in this pathway, from Burkholderia cenocepacia. HldA is structurally similar to members of the PfkB carbohydrate kinase family and appears to catalyze heptose phosphorylation via an in-line mechanism mediated mainly by a conserved aspartate, Asp270. Moreover, we report the structures of HldA in complex with two potent inhibitors in which both inhibitors adopt a folded conformation and occupy the nucleotide-binding sites. Together, these results provide important insight into the mechanism of HldA-catalyzed heptose phosphorylation and necessary information for further development of HldA inhibitors.
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Structural-Functional Studies of Burkholderia cenocepaciad-Glycero-beta-d-manno-heptose 7-Phosphate Kinase (HldA) and Characterization of Inhibitors with Antibiotic Adjuvant and Antivirulence Properties.,Lee TW, Verhey TB, Antiperovitch PA, Atamanyuk D, Desroy N, Oliveira C, Denis A, Gerusz V, Drocourt E, Loutet SA, Hamad MA, Stanetty C, Andres SN, Sugiman-Marangos S, Kosma P, Valvano MA, Moreau F, Junop MS J Med Chem. 2013 Jan 22. PMID:23256532<ref>PMID:23256532</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4e8y" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

Crystal Structure of Burkholderia cenocepacia HldA in Complex with an ATP-competitive Inhibitor

PDB ID 4e8y

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