title: The tail of mycolic acids.
abstract: The FabH enzyme from M. tuberculosis binds the acyl tail of large substrates at the end of a buried hydrophobic tunnel. Sachdeva et al. (2008) use reactive chemical probes and X-ray crystallography to show that substrates can bind to an open state of FabH without threading through the tunnel.
authors.affiliation: Department of Molecular Microbiology and Immunology, Johns Hopkins Bloomberg School of Public Health, 615 N. Wolfe Street, Baltimore, MD 21205, USA.
authors.forename: Jeff Zhiqiang
authors.initials: JZ
authors.lastname: Lu
authors.forename: Sean T
authors.initials: ST
authors.lastname: Prigge
mesh_terms: D015099:3-Oxoacyl-(Acyl-Carrier-Protein) Synthase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D001665:Binding Sites; D003545:Cysteine / Q000378:metabolism; D008024:Ligands; D008954:Models, Biological; D009154:Mutation; D009169:Mycobacterium tuberculosis / Q000201:enzymology*; D009171:Mycolic Acids / Q000378:metabolism*; D011485:Protein Binding
chemical_list: D008024:Ligands; D009171:Mycolic Acids; D015099:3-Oxoacyl-(Acyl-Carrier-Protein) Synthase; D003545:Cysteine