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 -- Data Supplement - Supporting Information -- Proceedings of the National Academy of Sciences

Supporting information for Márquez et al. (2002) Proc. Natl. Acad. Sci. USA 99 (6), 3458–3463. (10.1073/pnas.052461499)

Note 1.
A search with the program DALI (38) indicated significant similarity (score 4.2) with the archaeal thermosome (42) and with the a/b sub-domain from EI of the PTS system (43, 44), but not with its HPr binding domain (45). A somewhat lower score is returned for MurF (score 3.7), a protein involved in the synthesis of bacterial cell wall components (46). The similarity of HPrK with MurF extends over the whole N-terminal domain (residues 1-130), whereas enzyme I superimposes reasonably only on residues 13 to 118 of HPrK_N. In addition, the a/b sub-domain of enzyme I has a big a-helical insertion responsible for the interaction with the HPr protein which is absent in HPrK_N.