2hro
From Proteopedia
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'''Structure of the full-lenght Enzyme I of the PTS system from Staphylococcus carnosus''' | '''Structure of the full-lenght Enzyme I of the PTS system from Staphylococcus carnosus''' | ||
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[[Category: Reinelt, S.]] | [[Category: Reinelt, S.]] | ||
[[Category: Scheffzek, K.]] | [[Category: Scheffzek, K.]] | ||
| - | [[Category: | + | [[Category: Histidine phosphorylation]] |
| - | [[Category: | + | [[Category: Protein phosphorylation]] |
| - | [[Category: | + | [[Category: Pt]] |
| - | [[Category: | + | [[Category: Sugar transport]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:37:53 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 03:37, 4 May 2008
Structure of the full-lenght Enzyme I of the PTS system from Staphylococcus carnosus
Overview
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 2.5A reveals an extensive interaction surface between two molecules in adjacent asymmetric units. Structural comparison with related domains indicates that this surface represents the biochemically relevant contact area of dimeric EI. Each monomer has an extended configuration with the phosphohistidine and heat-stable phospho carrier protein-binding domains clearly separated from the C-terminal dimerization and PEP-binding region. The large distance of more than 35A between the active site His-190 and the PEP binding site suggests that large conformational changes must occur during the process of autophosphorylation, as has been proposed for the structurally related enzyme pyruvate phosphate dikinase. Our structure for the first time offers a framework to analyze a large amount of research in the context of the full-length model.
About this Structure
2HRO is a Single protein structure of sequence from Staphylococcus carnosus. Full crystallographic information is available from OCA.
Reference
Structure of the full-length enzyme I of the phosphoenolpyruvate-dependent sugar phosphotransferase system., Marquez J, Reinelt S, Koch B, Engelmann R, Hengstenberg W, Scheffzek K, J Biol Chem. 2006 Oct 27;281(43):32508-15. Epub 2006 Jul 25. PMID:16867985 Page seeded by OCA on Sun May 4 06:37:53 2008
