Literature summary for 2.7.1.71 extracted from

Dias, M.V.; Faim, L.M.; Vasconcelos, I.B.; Simoes de Oliveira, J.; Basso, L.A.; Santos, D.S.; Filgueira de Azevedo, W.J.
Effects of the magnesium and chloride ions and shikimate on the structure of shikimate kinase from Mycobacterium tuberculosis (2007), Acta Crystallogr. Sect. F, F63, 1-6.

Cloned(Commentary)

Cloned (Comment)	Organism
-	Mycobacterium tuberculosis

Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging drop vapour diffusion method, enzyme in complex with ADP and shikimate in the absence of Mg2+ using 0.1 M Tris-HCl buffer pH 8.0, 17% PEG 1500 and 0.5-0.7 M LiCl, or enzyme in complex with ADP and Mg2+ in the absence of shikimate using 0.1 M Tris-HCl buffer pH 8.0, 20% PEG 3350 and 0.1 M MgCl2*6H2O	Mycobacterium tuberculosis
in complex with ADP-shikimate and with MgADP-, at 1.93 A and 2.8 A resolution, respectively. Presence of Mg2+ influences the conformation of the shikimate hydroxyl groups and the position of the side chains of some of the residues of the activesite. Presence of Cl- seems to influence the affinity of ADP and its position in the active site and the opening length of the LID domain. Shikimate binding causes a closing of the LID domain and also seems to influence the crystallographic packing	Mycobacterium tuberculosis

Crystallization (Comment)

Organism

hanging drop vapour diffusion method, enzyme in complex with ADP and shikimate in the absence of Mg2+ using 0.1 M Tris-HCl buffer pH 8.0, 17% PEG 1500 and 0.5-0.7 M LiCl, or enzyme in complex with ADP and Mg2+ in the absence of shikimate using 0.1 M Tris-HCl buffer pH 8.0, 20% PEG 3350 and 0.1 M MgCl2*6H2O

Mycobacterium tuberculosis

in complex with ADP-shikimate and with MgADP-, at 1.93 A and 2.8 A resolution, respectively. Presence of Mg2+ influences the conformation of the shikimate hydroxyl groups and the position of the side chains of some of the residues of the activesite. Presence of Cl- seems to influence the affinity of ADP and its position in the active site and the opening length of the LID domain. Shikimate binding causes a closing of the LID domain and also seems to influence the crystallographic packing

Mycobacterium tuberculosis

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Cl-	increases the stability of the structure of the enzyme and influences the affinity of ADP for shikimate kinase	Mycobacterium tuberculosis
Mg2+	influences the position of the hydroxyl groups of the shikimate molecule and some of the residues of the active site of the enzyme	Mycobacterium tuberculosis

Organism

Organism	UniProt	Comment	Textmining
Mycobacterium tuberculosis	P9WPY3	-	-
Mycobacterium tuberculosis H37Rv	P9WPY3	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Mycobacterium tuberculosis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + shikimate	-	Mycobacterium tuberculosis	ADP + shikimate 3-phosphate	-	?
ATP + shikimate	-	Mycobacterium tuberculosis H37Rv	ADP + shikimate 3-phosphate	-	?

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Mycobacterium tuberculosis