Literature summary for 2.6.1.16 extracted from

Mouilleron, S.; Badet-Denisot, M.A.; Golinelli-Pimpaneau, B.
Ordering of C-terminal loop and glutaminase domains of glucosamine-6-phosphate synthase promotes sugar ring opening and formation of the ammonia channel (2008), J. Mol. Biol., 377, 1174-1185.

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structures of enzyme alone and in complex with the glucosamine 6-phosphate product at 2.95 A and 2.9 A resolution, respectively. No electron density for the glutaminase domain is observed. Upon sugar binding, the C-terminal loop, which forms the major part of the channel walls, becomes ordered and covers the synthase site. The ordering of the glutaminase domains likely follows fructose 6-phosphate binding by the anchoring of Trp74, which acts as the gate of the channel, on the closed C-terminal loop. This is accompanied by a major conformational change of the side chain of Lys503 of the neighboring synthase domain that strengthens the interactions of the synthase domain with the C-terminal loop and completely shields the synthase site. The concomitant conformational change of theLys503-Gly505 tripeptide places catalytic His504 in the proper position to open the sugar and buries the linear sugar, which is now in the vicinity of the catalytic groups involved in the sugar isomerization reaction	Escherichia coli

Crystallization (Comment)

Organism

crystal structures of enzyme alone and in complex with the glucosamine 6-phosphate product at 2.95 A and 2.9 A resolution, respectively. No electron density for the glutaminase domain is observed. Upon sugar binding, the C-terminal loop, which forms the major part of the channel walls, becomes ordered and covers the synthase site. The ordering of the glutaminase domains likely follows fructose 6-phosphate binding by the anchoring of Trp74, which acts as the gate of the channel, on the closed C-terminal loop. This is accompanied by a major conformational change of the side chain of Lys503 of the neighboring synthase domain that strengthens the interactions of the synthase domain with the C-terminal loop and completely shields the synthase site. The concomitant conformational change of theLys503-Gly505 tripeptide places catalytic His504 in the proper position to open the sugar and buries the linear sugar, which is now in the vicinity of the catalytic groups involved in the sugar isomerization reaction

Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P17169	-	-

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Release 2023.1 (January 2023)