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The structures of formylglycinamide ribonucleotide amidotransferase from S. typhimurium either with an unliganded glutaminase domain or in complex with an ATP analogue revealed that no major conformational changes take place upon formation of the glutamyl thioester intermediate or subsequent ATP complexation; therefore, formylglycinamide ribonucleotide binding is proposed to be the mechanism of activation of catalytic coupling in the enzyme.

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Three crystal structures of a lipoprotein (Bmlp7) of unknown function, a member of the 30 kDa lipoprotein family from mulberry silkworm (B. mori L.) haemolymph, have been determined. The haemolymph-isolated protein was identified through successful sequence assignment according to electron-density maps at 1.33 Å resolution.
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