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dc.contributor.authorBernardo-García, Noelia
dc.contributor.authorBartual, Sergio G
dc.contributor.authorFulde, Marcus
dc.contributor.authorBergmann, Simone
dc.contributor.authorHermoso, Juan A
dc.date.accessioned2012-08-02T11:44:02Z
dc.date.available2012-08-02T11:44:02Z
dc.date.issued2011-10-01
dc.identifier.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.en_GB
dc.identifier.issn1744-3091
dc.identifier.pmid22102049
dc.identifier.doi10.1107/S1744309111030922
dc.identifier.urihttp://hdl.handle.net/10033/237024
dc.description.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.
dc.language.isoenen
dc.rightsArchived with thanks to Acta crystallographica. Section F, Structural biology and crystallization communicationsen_GB
dc.subject.meshCrystallizationen_GB
dc.subject.meshCrystallography, X-Rayen_GB
dc.subject.meshPhosphoglycerate Kinaseen_GB
dc.subject.meshStreptococcus pneumoniaeen_GB
dc.titleCrystallization and preliminary X-ray diffraction analysis of phosphoglycerate kinase from Streptococcus pneumoniae.en
dc.typeArticleen
dc.contributor.departmentDepartment of Crystallography and Structural Biology, Instituto de Química-Física Rocasolano, CSIC, Serrano 119, 28006 Madrid, Spain.en_GB
dc.identifier.journalActa crystallographica. Section F, Structural biology and crystallization communicationsen_GB
refterms.dateFOA2018-06-12T21:27:38Z
html.description.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.


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