Müller Peter, Sawaya Michael R, Pashkov Inna, Chan Sum, Nguyen Chau, Wu Yim, Perry L Jeanne, Eisenberg David
UCLA-DOE Institute for Genomics and Proteomics, Howard Hughes Medical Institute, Box 951570, Los Angeles, CA 90095-1570, USA.
Acta Crystallogr D Biol Crystallogr. 2005 Mar;61(Pt 3):309-15. doi: 10.1107/S0907444904033190. Epub 2005 Feb 24.
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.
结核分枝杆菌磷酸甘油酸变位酶的单晶X射线结构已在1.70埃的分辨率下测定。每个亚基的C末端尾巴是灵活且无序的；然而，对于四条链中的一条链（A链），除了五个残基外，该链的其余部分都可以进行建模。该结构的显著特征包括活性位点以及每个单体中富含脯氨酸的片段形成一个短的左手多聚脯氨酰螺旋。这些片段位于酶的表面，可以想象它们参与蛋白质-蛋白质相互作用。
