The 1.70 angstroms X-ray crystal structure of Mycobacterium tuberculosis phosphoglycerate mutase

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 chai...

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Bibliographic Details
Published in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2005-03, Vol.61 (Pt 3), p.309-315
Main Authors: Müller, Peter, Sawaya, Michael R, Pashkov, Inna, Chan, Sum, Nguyen, Chau, Wu, Yim, Perry, L Jeanne, Eisenberg, David
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Base Sequence
Binding Sites
Crystallography, X-Ray
DNA Primers
Models, Molecular
Molecular Sequence Data
Mycobacterium tuberculosis - enzymology
Phosphoglycerate Mutase - chemistry
Protein Conformation
Protein Folding
Sequence Homology, Amino Acid
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Summary: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.
ISSN:0907-4449