4lkv

<StructureSection load='4lkv' size='340' side='right' caption='[[4lkv]], [[Resolution|resolution]] 3.51&Aring;' scene=''>

<table><tr><td colspan='2'>[[4lkv]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LKV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LKV FirstGlance]. <br>

</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=LP4:2-DEOXY-3-O-[(3R)-3-HYDROXYTETRADECANOYL]-2-{[(3R)-3-HYDROXYTETRADECANOYL]AMINO}-4-O-PHOSPHONO-BETA-D-GLUCOPYRANOSE'>LP4</scene>, <scene name='pdbligand=LP5:(R)-((2R,3S,4R,5R,6R)-3-HYDROXY-2-(HYDROXYMETHYL)-5-((R)-3-HYDROXYTETRADECANAMIDO)-6-(PHOSPHONOOXY)TETRAHYDRO-2H-PYRAN-4-YL)+3-HYDROXYTETRADECANOATE'>LP5</scene><br>

<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ehw|4ehw]], [[4ehx|4ehx]], [[4ehy|4ehy]], [[4itl|4itl]], [[4itm|4itm]], [[4itn|4itn]]</td></tr>

<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tetraacyldisaccharide_4'-kinase Tetraacyldisaccharide 4'-kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.130 2.7.1.130] </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>

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== 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>

 

[[Category: Tetraacyldisaccharide 4'-kinase]]

[[Category: Emptage, R P.]]

[[Category: Schumacher, M A.]]

[[Category: Tonthat, N K.]]

[[Category: York, J D.]]

[[Category: Zhou, P.]]

[[Category: Membrane protein]]

[[Category: P-loop containing nucleotide triphosphate hydrolase]]

[[Category: Transferase]]