2006
DOI: 10.1074/jbc.m513721200
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Structure of the Full-length Enzyme I of the Phosphoenolpyruvate-dependent Sugar Phosphotransferase System

Abstract: Enzyme I (EI) is the phosphoenolpyruvate (PEP)-protein phosphotransferase at the entry point of the PEP-dependent sugar phosphotransferase system, which catalyzes carbohydrate uptake into bacterial cells. In the first step of this pathway EI phosphorylates the heat-stable phospho carrier protein at His-15 using PEP as a phosphoryl donor in a reaction that requires EI dimerization and autophosphorylation at His-190. The structure of the full-length protein from Staphylococcus carnosus at 2.5 Å reveals an extens… Show more

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Cited by 26 publications
(55 citation statements)
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References 46 publications
(65 reference statements)
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“…While this article was being reviewed, the crystal structure of apo-EI from Staphylococcus carnosus was published (46). The His domain in this structure is largely disordered; however, the helical linker is defined and confirms our swiveling domain hypothesis.…”
Section: Results and Discussion Eimentioning
confidence: 71%
“…While this article was being reviewed, the crystal structure of apo-EI from Staphylococcus carnosus was published (46). The His domain in this structure is largely disordered; however, the helical linker is defined and confirms our swiveling domain hypothesis.…”
Section: Results and Discussion Eimentioning
confidence: 71%
“…The first conformational state is optimal for the phosphotransfer reaction between EIN and HPr, and the second conformational state is relevant for the autophosphorylation reaction between EIN and EIC. [8][9][10] Isolated EIN adopts predominantly the first conformational state in solution, but the interaction with EIC requires a switch to the second conformational state. 5 Fig.…”
Section: Resultsmentioning
confidence: 99%
“…The linker region forms a long helix from residue Thr232 to residue Lys257, followed by a short b bridge (Ala261-Val269) that connects the linker helix to the (ab) 8 barrel fold of EIC. The EIC 231-575 construct contains the linker helix followed by EIC, whereas the EIC 260-575 construct lacks the whole linker helix.…”
Section: Resultsmentioning
confidence: 99%
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