2.7.7.23	-	643075, 643076	
2.7.7.23	a 1.9 A resolution crystal structure of a synthetic small-molecule inhibitor (4-chloro-N-(3-methoxypropyl)-N-[1-(2-phenylethyl)piperidin-3-yl]benzamide) of GlmU is presented. The determined crystal structure indicate that the inhibitor occupies an allosteric site adjacent to the GlcNAc-1-P substrate-binding region, thus, preventing structural rearrangements that are required for the enzymatic reaction	706622	
2.7.7.23	apo GlmU is crystallized at 20 °C using the sitting-drop vapor diffusion methodcrystal structure of a mimic of the Michaelis complex, with glucose 1-phosphate and acetyl-coenzyme A, helps us to propose the residues involved in deprotonation of glucosamine 1-phosphate and the loop movement that likely generates the active site required for glucosamine 1-phosphate to bind	756049	
2.7.7.23	generation of a three-dimensional model, using human GlcNAc1p nucleotidyltransferase complexed with UDP-GlcNAc, PDB code 1JV1	721526	
2.7.7.23	GlmUMtb active site crystal structure analysis, PDB ID 3DJ4, and crystal structure of GlmU with both substrates (i.e., GlcNAc-1-P and UTP) in the presence of metal ions, soaking of GlmUMtb[Apo] crystals in a solution containing GlcNAc-1-P, UTP and MgCl2. the soaking solution consists of 10% PEG 8000, 100 mM HEPES, pH 7.5, 20 mM MgCl2, and 4 mM CoCl2, and substrate 50 mM GlcNAc-1-phosphate, with or without 10 mM UTP, for 4 h at 4°C, X-ray diffraction structure determination and analysis at 2.0 A resolution using molecular replacement with GlmUMtb[Apo] as a search model	740866	
2.7.7.23	GlmUMtb in complex with substrates/products bound at the acetyltransferase active site, sitting drop vapor diffusion method, mixing of 400 nl of 15 mg/ml protein, 5 mM acetyl-CoA, 5 mM MgCl2, 5 mM UDP-GlcNAc with 400 nl of 18% PEG 3350, 0.1 M Tris-Cl, pH 8.5, and 2% tacsimate, 4-8 days, for enzyme complex with CoA and N-acetylglucosamine-1-phosphate, acetyl-Coa-containing crystals are soaked in 5 mM GlcN-1-P, 5 mM MgCl2, 5 mM UDP-GlcNAc, 5 mM acetyl-CoA, 18% PEG 3350, 0.1 M Tris-Cl, pH 8.5, and 2% tacsimate, or by co-crystallizing the enzyme with 5 mM GlcNAc-1-P, 5 mM MgCl2, 5 mM UDPGlcNAc, and 5 mM CoA under the conditions mentioned for obtaining GlmUMtb(AcCoA) crystals, X-ray diffraction structure determination and analysis at 1.98-2.33 A resolution	720042	
2.7.7.23	hanging drop vapour diffusion method	674815	
2.7.7.23	hanging drop vapour diffusion method, using 20% PEG 3350, 0.15 M DL-malate pH 7.0	690292	
2.7.7.23	homology modeling of structure based on Haemophilus influenzae enzyme, PDB entry 2V0K	719411	
2.7.7.23	in complex with inhibitor 3-[2-(1,3-benzodioxol-5-yl)-2-oxoethyl]-4-bromo-3-hydroxy-5-methyl-1,3-dihydro-2H-indol-2-one. Only the (R)-enantiomer binds, and it is likely that the kinked shape of the molecule is crucial for its shape-complimentarity to the pocket. The benzo[1,3]dioxole moiety is deeply buried, making close contact with Ala397 and Gly232 at the bottom of the cleft. The indolin-2-one sits at the top of the cleft, with the unsubstituted edge exposed to solvent and the methyl and bromide substituents on making contact with Ala239, Met370, Lys371, and Ala367	737319