Literature summary for 1.1.98.3 extracted from

Batt, S.M.; Jabeen, T.; Bhowruth, V.; Quill, L.; Lund, P.A.; Eggeling, L.; Alderwick, L.J.; Fuetterer, K.; Besra, G.S.
Structural basis of inhibition of Mycobacterium tuberculosis DprE1 by benzothiazinone inhibitors (2012), Proc. Natl. Acad. Sci. USA, 109, 11354-11359.

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Mycobacterium tuberculosis

Crystallization (Commentary)

Crystallization (Comment)	Organism
different crystal forms of ligand-free enzyme reveal considerable levels of structural flexibility of two surface loops that seem to govern accessibility of the active site. Structures of complexes with the benzothiazinone-derived nitroso derivative 3-nitroso-N-[(1R)-1-phenylethyl]-5-(trifluoromethyl)benzamide reveal that inhibitor binding includes a covalent link to conserved Cys387, and reveal a trifluoromethyl group as a second key determinant of interaction with the enzyme. A noncovalent complex is formed between the enzyme and 3-nitro-N-[(1R)-1-phenylethyl]-5-(trifluoromethyl)benzamide, which is structurally identical to 3-nitroso-N-[(1R)-1-phenylethyl]-5-(trifluoromethyl)benzamide except for an inert nitro group replacing the reactive nitroso group. Binding of benzothiazinone-class inhibitors to the enzyme is not strictly dependent on formation of the covalent link to Cys387	Mycobacterium tuberculosis

Crystallization (Comment)

Organism

different crystal forms of ligand-free enzyme reveal considerable levels of structural flexibility of two surface loops that seem to govern accessibility of the active site. Structures of complexes with the benzothiazinone-derived nitroso derivative 3-nitroso-N-[(1R)-1-phenylethyl]-5-(trifluoromethyl)benzamide reveal that inhibitor binding includes a covalent link to conserved Cys387, and reveal a trifluoromethyl group as a second key determinant of interaction with the enzyme. A noncovalent complex is formed between the enzyme and 3-nitro-N-[(1R)-1-phenylethyl]-5-(trifluoromethyl)benzamide, which is structurally identical to 3-nitroso-N-[(1R)-1-phenylethyl]-5-(trifluoromethyl)benzamide except for an inert nitro group replacing the reactive nitroso group. Binding of benzothiazinone-class inhibitors to the enzyme is not strictly dependent on formation of the covalent link to Cys387

Mycobacterium tuberculosis

Inhibitors

Inhibitors	Comment	Organism	Structure
3-nitro-N-[(1R)-1-phenylethyl]-5-(trifluoromethyl)benzamide	forms a noncovalent complex with the enzyme	Mycobacterium tuberculosis
3-nitroso-N-[(1R)-1-phenylethyl]-5-(trifluoromethyl)benzamide	benzothiazinone-derived inhibitor, binding includes a covalent link to conserved Cys387, and trifluoromethyl group is a second key determinant of interaction with the enzyme	Mycobacterium tuberculosis

Organism

Organism	UniProt	Comment	Textmining
Mycobacterium tuberculosis	P9WJF1	-	-
Mycobacterium tuberculosis H37Rv	P9WJF1	-	-