Correction: Organism-Adapted Specificity of the Allosteric Regulation of Pyruvate Kinase in Lactic Acid Bacteria
Publication year - 2014
Publication title -
plos computational biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.628
H-Index - 182
eISSN - 1553-7358
pISSN - 1553-734X
DOI - 10.1371/journal.pcbi.1003732
Subject(s) - pyruvate kinase , lactic acid , allosteric regulation , organism , bacteria , computational biology , biochemistry , biology , genetics , glycolysis , enzyme
There is an error in the nomenclature of one compound studied in this paper. The phosphate moieties of fructose 1,6-bisphosphate (FBP) were incorrectly labelled with the 1’-phosphate being labelled 6’ and the 6’-phosphate being labelled 1’. The corrected figure legend and sentences are: In Results/Discussion, Section ‘‘PYKs show a conserved phosphate binding site in the allosteric activator binding site’’, paragraph 1, 8th sentence: The phosphate interaction sites that coincide with the 69-phosphate and the 19-phosphate moieties of FBP are labelled 19Pibs and 69Pibs, respectively. In Results/Discussion, Section ‘‘Lactic acid bacteria PYKs lack a second phosphate binding site in the activator binding site’’, paragraph 1, 2nd sentence: In the yeast and the human M2-type PYKs, the side chains of tryptophan (W452 in 1A3W and W482 in 3GR4) and arginine (R459 in 1A3W and R489 in 3GR4) residues are computed to interact with the 19-phosphate moiety of FBP (see Figure 1).
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom