1A3A

CRYSTAL STRUCTURE OF IIA MANNITOL FROM ESCHERICHIA COLI

Summary for 1A3A

• Entry DOI: 10.2210/pdb1a3a/pdb
• Descriptor: MANNITOL-SPECIFIC EII (2 entities in total)
• Functional Keywords: phosphoenolpyruvate dependent phosphotransferase system, iia enzymes, histidine phosphorylation, phosphotransferase
• Biological source: Escherichia coli
• Cellular location: Cell inner membrane; Multi-pass membrane protein: P00550
• Total number of polymer chains: 4
• Total formula weight: 65394.19

Authors

Van Montfort, R.L.M.,Pijning, T.,Kalk, K.H.,Hangyi, I.,Kouwijzer, M.L.C.E.,Robillard, G.T.,Dijkstra, B.W. (deposition date: 1998-01-19, release date: 1998-08-12, Last modification date: 2024-02-07)

Primary citation

van Montfort, R.L.,Pijning, T.,Kalk, K.H.,Hangyi, I.,Kouwijzer, M.L.,Robillard, G.T.,Dijkstra, B.W.
The structure of the Escherichia coli phosphotransferase IIAmannitol reveals a novel fold with two conformations of the active site.
Structure, 6:377-388, 1998

PubMed Abstract: The bacterial phosphoenolpyruvate-dependent phosphotransferase system (PTS) catalyses the cellular uptake and subsequent phosphorylation of carbohydrates. Moreover, the PTS plays a crucial role in the global regulation of various metabolic pathways. The PTS consists of two general proteins, enzyme I and the histidine-containing protein (HPr), and the carbohydrate-specific enzyme II (EII). EIIs are usually composed of two cytoplasmic domains, IIA and IIB, and a transmembrane domain, IIC. The IIA domains catalyse the transfer of a phosphoryl group from HPr to IIB, which phosphorylates the transported carbohydrate. Knowledge of the structures of the IIA proteins may provide insight into the mechanisms by which the PTS couples phosphorylation reactions with carbohydrate specificity.

PubMed: 9551558
DOI: 10.1016/S0969-2126(98)00039-2

Experimental method

X-RAY DIFFRACTION (1.8 Å)