X-RAY CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS BETA-KETOACYL-ACYL CARRIER PROTEIN SYNTHASE III (MTFABH)X-RAY CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS BETA-KETOACYL-ACYL CARRIER PROTEIN SYNTHASE III (MTFABH)
Structural highlights
1m1m is a 2 chain structure with sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
FABH_MYCTU Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for long chain acyl-CoA such as myristoyl-CoA. Does not use acyl-CoA as primer. Its substrate specificity determines the biosynthesis of mycolic acid fatty acid chain, which is characteristic of mycobacterial cell wall.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
