EC Number   |
Reference  |
|---|
   2.7.8.43 | purified recombinant His-tagged wild-type and selenomethionine-labeled enzyme EptC, sitting drop vapour diffusion method, mixing of 0.004 ml of 30 mg/ml protein in 25 mM NaCl, 10 mM HEPES, pH 7.5, with 0.001 ml of precipitant solution containing 200 mM diammonium phosphate, 15% w/v PEG 3350, 22°C, X-ray diffraction structure determination and analysis at 2.40-2.80 A resolution, molecular replacement |
739786 |
| 2.7.8.43 | purified recombinant His6-tagged soluble catalytic domain of LptA, free and selenomethionine-labeled, or in complex with Zn2+ and a truncated form of substrate 1,2-dihexanoyl-sn-glycero-3-phosphoethanolamine, X-ray diffraction structure determination and analysis at 1.43-1.78 A resolution, molecular replacement. and modeling |
734476 |
| 2.7.8.43 | recombinant His-tagged membrane-deletion mutant enzyme, mixing of 0.001 ml of 5.2 mg/ml protein in 50 mM HEPES, pH 8.0, 50 mM sodium chloride, with 0.001 ml of crystallization solution containing 23-26% PEG 8000, 100 mM ammonium sulfate, 100 mM HEPES, pH 7.58.0, 15 mM n-dodecyl-N,N-dimethylamine-N-oxide, and 200 nl of microseeding solution, 20°C, 3-5 days, method optimization, X-ray diffraction structure determination and analysis at 1.7 A resolution |
733017 |
| 2.7.8.43 | structure of full-length lipid A phosphoethanolamine transferase, determined to 2.75 A resolution. The structure reveals a helical membrane domain and a periplasmic facing soluble domain. The domains are linked by a helix that runs along the membrane surface interacting with the phospholipid head groups. Two helices located in a periplasmic loop between two transmembrane helices contain conserved charged residues and are implicated in substrate binding |
762273 |
| 2.7.8.43 | structure of the catalytic domain of ICR.. Catalytic domain dimerization is required for substrate binding. The structure reveals two disulfide bonds (Cys390 to Cys398, Cys448 to Cys456) |
760257 |
| 2.7.8.43 | structure of the catalytic domain ofMCR1 at 1.32 A resolution. The putative nucleophile for catalysis, threonine 285, is phosphorylated in MCR1 and a zinc is present at a conserved site in addition to three zincs more peripherally located in the active site. Binding sites for the lipid A and phosphatidylethanolamine substrates are not apparent in the MCR1 structure |
760783 |
