Crystallization and preliminary X-ray diffraction analysis of phosphoglycerate kinase from Streptococcus pneumoniae.
Cast your vote
You can rate an item by clicking the amount of stars they wish to award to this item.
When enough users have cast their vote on this item, the average rating will also be shown.
Your vote was cast
Thank you for your feedback
Thank you for your feedback
MetadataShow full item record
AbstractPhosphoglycerate kinase (PGK) is a widespread two-domain enzyme that plays a critical role in the glycolytic pathway. Several glycolytic enzymes from streptococci have been identified as surface-exposed proteins that are involved in streptococcal virulence by their ability to bind host proteins. This binding allows pneumococcal cells to disseminate through the epithelial and endothelial layers. Crystallization of PGK from Streptococcus pneumoniae yielded orthorhombic crystals (space group I222, unit-cell parameters a = 62.73, b = 75.38, c = 83.63 Å). However, the unit cell of these crystals was not compatible with the presence of full-length PGK. Various analytical methods showed that only the N-terminal domain of PGK was present in the I222 crystals. The ternary complex of PGK with adenylyl imidodiphosphate (AMP-PNP) and 3-phospho-D-glycerate (3PGA) produced monoclinic crystals (space group P2(1), unit-cell parameters a = 40.35, b = 78.23, c = 59.03 Å, β = 96.34°). Molecular replacement showed that this new crystal form contained full-length PGK, thereby indicating the relevance of including substrates in order to avoid proteolysis during the crystallization process.
CitationCrystallization and preliminary X-ray diffraction analysis of phosphoglycerate kinase from Streptococcus pneumoniae. 2011, 67 (Pt 10):1285-9 Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.
AffiliationDepartment of Crystallography and Structural Biology, Instituto de Química-Física Rocasolano, CSIC, Serrano 119, 28006 Madrid, Spain.
The following license files are associated with this item:
- Crystallization and preliminary X-ray analysis of a bacterial psychrophilic enzyme, phosphoglycerate kinase.
- Authors: Mandelman D, Bentahir M, Feller G, Gerday C, Haser R
- Issue date: 2001 Nov
- Purification, crystallization and preliminary X-ray analysis of the 3-phosphoglycerate kinase from Bacillus stearothermophilus.
- Authors: Davies GJ, Gamblin SJ, Littlechild JA, Watson HC
- Issue date: 1992 Oct 20
- Crystal structures of substrates and products bound to the phosphoglycerate kinase active site reveal the catalytic mechanism.
- Authors: Bernstein BE, Hol WG
- Issue date: 1998 Mar 31
- Structure of the R65Q mutant of yeast 3-phosphoglycerate kinase complexed with Mg-AMP-PNP and 3-phospho-D-glycerate.
- Authors: McPhillips TM, Hsu BT, Sherman MA, Mas MT, Rees DC
- Issue date: 1996 Apr 2
- The importance of dynamic light scattering in obtaining multiple crystal forms of Trypanosoma brucei PGK.
- Authors: Bernstein BE, Michels PA, Kim H, Petra PH, Hol WG
- Issue date: 1998 Feb