1ZYM

AMINO TERMINAL DOMAIN OF ENZYME I FROM ESCHERICHIA COLI

Summary for 1ZYM

• Entry DOI: 10.2210/pdb1zym/pdb
• Descriptor: ENZYME I (2 entities in total)
• Functional Keywords: phosphotransferase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P08839
• Total number of polymer chains: 2
• Total formula weight: 56448.24

Authors

Liao, D.-I.,Davies, D.R. (deposition date: 1996-05-21, release date: 1996-12-07, Last modification date: 2024-02-14)

Primary citation

Liao, D.I.,Silverton, E.,Seok, Y.J.,Lee, B.R.,Peterkofsky, A.,Davies, D.R.
The first step in sugar transport: crystal structure of the amino terminal domain of enzyme I of the E. coli PEP: sugar phosphotransferase system and a model of the phosphotransfer complex with HPr.
Structure, 4:861-872, 1996

PubMed Abstract: The bacterial phosphoenolpyruvate (PEP): sugar phosphotransferase system (PTS) transports exogenous hexose sugars through the membrane and tightly couples transport with phosphoryl transfer from PEP to the sugar via several phosphoprotein intermediates. The phosphate group is first transferred to enzyme I, second to the histidine-containing phosphocarrier protein HPr, and then to one of a number of sugar-specific enzymes II. The structures of several HPrs and enzymes IIA are known. Here we report the structure of the N-terminal half of enzyme I from Escherichia coli (EIN).

PubMed: 8805571
DOI: 10.1016/S0969-2126(96)00092-5

Experimental method

X-RAY DIFFRACTION (2.5 Å)