{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["99(6)"],"submitter":["Marquez JA"],"pubmed_abstract":["The histidine containing phospho carrier protein (HPr) kinase/phosphatase is involved in carbon catabolite repression, mainly in Gram-positive bacteria. It is a bifunctional enzyme that phosphorylates Ser-46-HPr in an ATP-dependent reaction and dephosphorylates P-Ser-46-HPr. X-ray analysis of the full-length crystalline enzyme from Staphylococcus xylosus at a resolution of 1.95 A shows the enzyme to consist of two clearly separated domains that are assembled in a hexameric structure resembling a three-bladed propeller. The N-terminal domain has a betaalphabeta fold similar to a segment from enzyme I of the sugar phosphotransferase system and to the uridyl-binding portion of MurF; it is structurally organized in three dimeric modules exposed to form the propeller blades. Two unexpected phos"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pagination":["3458-63"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC122545"],"repository":["biostudies-literature"],"pubmed_title":["Structure of the full-length HPr kinase/phosphatase from Staphylococcus xylosus at 1.95 A resolution: Mimicking the product/substrate of the phospho transfer reactions."],"pmcid":["PMC122545"],"pubmed_authors":["Hengstenberg W","Russell RB","Fieulaine S","Marquez JA","Hasenbein S","Koch B","Nessler S","Scheffzek K"],"additional_accession":[]},"is_claimable":false,"name":"Structure of the full-length HPr kinase/phosphatase from Staphylococcus xylosus at 1.95 A resolution: Mimicking the product/substrate of the phospho transfer reactions.","description":"The histidine containing phospho carrier protein (HPr) kinase/phosphatase is involved in carbon catabolite repression, mainly in Gram-positive bacteria. It is a bifunctional enzyme that phosphorylates Ser-46-HPr in an ATP-dependent reaction and dephosphorylates P-Ser-46-HPr. X-ray analysis of the full-length crystalline enzyme from Staphylococcus xylosus at a resolution of 1.95 A shows the enzyme to consist of two clearly separated domains that are assembled in a hexameric structure resembling a three-bladed propeller. The N-terminal domain has a betaalphabeta fold similar to a segment from enzyme I of the sugar phosphotransferase system and to the uridyl-binding portion of MurF; it is structurally organized in three dimeric modules exposed to form the propeller blades. Two unexpected phos","dates":{"release":"2002-01-01T00:00:00Z","publication":"2002 Mar","modification":"2026-03-31T11:28:30.051Z","creation":"2019-03-27T00:17:10Z"},"accession":"S-EPMC122545","cross_references":{"pubmed":["11904409"],"doi":["10.1073/pnas.052461499"]}}