2HWG

Structure of phosphorylated Enzyme I of the phosphoenolpyruvate:sugar phosphotransferase system

Summary for 2HWG

• Entry DOI: 10.2210/pdb2hwg/pdb
• Descriptor: Phosphoenolpyruvate-protein phosphotransferase, MAGNESIUM ION, OXALATE ION, ... (4 entities in total)
• Functional Keywords: enzyme i, phosphoenolpyruvate:sugar phosphotransferase system, pts, transferase
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 129342.14

Authors

Lim, K.,Teplyakov, A.,Herzberg, O. (deposition date: 2006-08-01, release date: 2006-11-14, Last modification date: 2023-11-15)

Primary citation

Teplyakov, A.,Lim, K.,Zhu, P.P.,Kapadia, G.,Chen, C.C.,Schwartz, J.,Howard, A.,Reddy, P.T.,Peterkofsky, A.,Herzberg, O.
Structure of phosphorylated enzyme I, the phosphoenolpyruvate:sugar phosphotransferase system sugar translocation signal protein.
Proc.Natl.Acad.Sci.Usa, 103:16218-16223, 2006

PubMed Abstract: Bacterial transport of many sugars, coupled to their phosphorylation, is carried out by the phosphoenolpyruvate (PEP):sugar phosphotransferase system and involves five phosphoryl group transfer reactions. Sugar translocation initiates with the Mg(2+)-dependent phosphorylation of enzyme I (EI) by PEP. Crystals of Escherichia coli EI were obtained by mixing the protein with Mg(2+) and PEP, followed by oxalate, an EI inhibitor. The crystal structure reveals a dimeric protein where each subunit comprises three domains: a domain that binds the partner PEP:sugar phosphotransferase system protein, HPr; a domain that carries the phosphorylated histidine residue, His-189; and a PEP-binding domain. The PEP-binding site is occupied by Mg(2+) and oxalate, and the phosphorylated His-189 is in-line for phosphotransfer to/from the ligand. Thus, the structure represents an enzyme intermediate just after phosphotransfer from PEP and before a conformational transition that brings His-189 approximately P in proximity to the phosphoryl group acceptor, His-15 of HPr. A model of this conformational transition is proposed whereby swiveling around an alpha-helical linker disengages the His domain from the PEP-binding domain. Assuming that HPr binds to the HPr-binding domain as observed by NMR spectroscopy of an EI fragment, a rotation around two linker segments orients the His domain relative to the HPr-binding domain so that His-189 approximately P and His-15 are appropriately stationed for an in-line phosphotransfer reaction.

PubMed: 17053069
DOI: 10.1073/pnas.0607587103

Experimental method

X-RAY DIFFRACTION (2.7 Å)