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4lkv
From Proteopedia
(Difference between revisions)
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4lkv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lkv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lkv RCSB], [http://www.ebi.ac.uk/pdbsum/4lkv PDBsum]</span></td></tr> | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4lkv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lkv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lkv RCSB], [http://www.ebi.ac.uk/pdbsum/4lkv PDBsum]</span></td></tr> | ||
<table> | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The membrane-bound tetraacyldisaccharide-1-phosphate kinase, LpxK, catalyzes the sixth step of the lipid A (Raetz) biosynthetic pathway and is a viable antibiotic target against emerging Gram-negative pathogens. We report the crystal structure of lipid IVA, the LpxK product, bound to the enzyme, providing a rare glimpse into interfacial catalysis and the surface scanning strategy by which many poorly understood lipid modification enzymes operate. Unlike the few previously structurally characterized proteins that bind lipid A or its precursors, LpxK binds almost exclusively to the glucosamine-phosphate moieties of the lipid molecule. Steady-state kinetic analysis of multiple point mutants of the lipid-binding pocket pinpoints critical residues involved in substrate binding, and characterization of N-terminal helix truncation mutants uncovers the role of this substructure as a hydrophobic membrane anchor. These studies make critical contributions to the limited knowledge surrounding membrane-bound enzymes that act upon lipid substrates and provide a structural template for designing small-molecule inhibitors targeting this essential kinase. | ||
| + | |||
| + | Structural basis of lipid binding for the membrane-embedded tetraacyldisaccharide-1-phosphate 4'-kinase LpxK.,Emptage RP, Tonthat NK, York JD, Schumacher MA, Zhou P J Biol Chem. 2014 Jul 14. pii: jbc.M114.589986. PMID:25023290<ref>PMID:25023290</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 06:33, 30 July 2014
Determinants of lipid substrate and membrane binding for the tetraacyldisaccharide-1-phosphate 4 -kinase LpxK
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