Homoserine transacetylase MetX from Mycobacterium tuberculosis

Structural analysis of mycobacterial homoserine transacetylases central to methionine biosynthesis reveals druggable active site.

ROSENBAUM-ROCK DOUBLE-CRYSTAL MONOCHROMATOR: LIQUID NITROGEN COOLED; SAGITALLY FOCUSING 2ND CRYSTAL, ROSENBAUM-ROCK VERTICAL FOCUSING MIRROR

GAMTLPAEGEIGLIDVGSLQLESGAVIDDVCIAVQRWGKLSPARDNVVVVLHALTGDSHITGPAGPGHPTPGWWDGVAGP
GAPIDTTRWCAVATNVLGGCRGSTGPSSLARDGKPWGSRFPLISIRDQVQADVAALAALGITEVAAVVGGSMGGARALEW
VVGYPDRVRAGLLLAVGARATADQIGTQTTQIAAIKADPDWQSGDYHETGRAPDAGLRLARRFAHLTYRGEIELDTRFAN
HNQGNEDPTAGGRYAVQSYLEHQGDKLLSRFDAGSYVILTEALNSHDVGRGRGGVSAALRACPVPVVVGGITSDRLYPLR
LQQELADLLPGCAGLRVVESVYGHDGFLVETEAVGELIRQTLGLAD

Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

0.1 M Tris-HCl, pH 8.5, 1.8 M Magnesium Sulfate

National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)

methionine biosynthesis, HOMOSERINE O-ACETYLTRANSFERASE, HOMOSERINE O-TRANSACETYLASE, HTA, MetX, Rv3341, TRANSFERASE

TLPAEGEIGLIDVGSLQLESGAVIDDVCIAVQRWGKLSPARDNVVVVLHALTGDSHITGPAGPGHPTPGWWDGVAGPGAP
IDTTRWCAVATNVLGGCRGSTGPSSLARDGKPWGSRFPLISIRDQVQADVAALAALGITEVAAVVGGSMGGARALEWVVG
YPDRVRAGLLLAVGARATADQIGTQTTQIAAIKADPDWQSGDYHETGRAPDAGLRLARRFAHLTYRGEIELDTRFANHNQ
GNEDPTAGGRYAVQSYLEHQGDKLLSRFDAGSYVILTEALNSHDVGRGRGGVSAALRACPVPVVVGGITSDRLYPLRLQQ
ELADLLPGCAGLRVVESVYGHDGFLVETEAVGELIRQTLGLAD