title: The 1.70 angstroms X-ray crystal structure of Mycobacterium tuberculosis phosphoglycerate mutase.
abstract: The single-crystal X-ray structure of phosphoglycerate mutase from Mycobacterium tuberculosis has been determined at a resolution of 1.70 angstroms. The C-terminal tail of each of the subunits is flexible and disordered; however, for one of the four chains (chain A) all but five residues of the chain could be modeled. Noteworthy features of the structure include the active site and a proline-rich segment in each monomer forming a short left-handed polyprolyl helix. These segments lie on the enzyme surface and could conceivably participate in protein-protein interactions.
authors.affiliation: UCLA-DOE Institute for Genomics and Proteomics, Howard Hughes Medical Institute, Box 951570, Los Angeles, CA 90095-1570, USA.
authors.forename: Peter
authors.initials: P
authors.lastname: Müller
authors.forename: Michael R
authors.initials: MR
authors.lastname: Sawaya
authors.forename: Inna
authors.initials: I
authors.lastname: Pashkov
authors.forename: Sum
authors.initials: S
authors.lastname: Chan
authors.forename: Chau
authors.initials: C
authors.lastname: Nguyen
authors.forename: Yim
authors.initials: Y
authors.lastname: Wu
authors.forename: L Jeanne
authors.initials: LJ
authors.lastname: Perry
authors.forename: David
authors.initials: D
authors.lastname: Eisenberg
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D001665:Binding Sites; D018360:Crystallography, X-Ray; D017931:DNA Primers; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009169:Mycobacterium tuberculosis / Q000201:enzymology*; D010736:Phosphoglycerate Mutase / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding; D017386:Sequence Homology, Amino Acid
chemical_list: D017931:DNA Primers; D010736:Phosphoglycerate Mutase