1TVM

NMR structure of enzyme GatB of the galactitol-specific phosphoenolpyruvate-dependent phosphotransferase system

Summary for 1TVM

• Entry DOI: 10.2210/pdb1tvm/pdb
• NMR Information: BMRB: 6259
• Descriptor: PTS system, galactitol-specific IIB component (1 entity in total)
• Functional Keywords: phosphotransferase system (pts), p-loop, four-stranded parallel open twisted beta sheet flanked by alpha helices on both sides, e. coli, montreal-kingston bacterial structural genomics initiative, bsgi, structural genomics, transferase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm (By similarity): Q8X7H5
• Total number of polymer chains: 1
• Total formula weight: 12481.33

Authors

Volpon, L.,Young, C.R.,Lim, N.S.,Iannuzzi, P.,Cygler, M.,Gehring, K.,Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) (deposition date: 2004-06-29, release date: 2005-09-06, Last modification date: 2024-05-22)

Primary citation

Volpon, L.,Young, C.R.,Matte, A.,Gehring, K.
NMR structure of the enzyme GatB of the galactitol-specific phosphoenolpyruvate-dependent phosphotransferase system and its interaction with GatA.
Protein Sci., 15:2435-2441, 2006

PubMed Abstract: The phosphoenolpyruvate-dependent carbohydrate transport system (PTS) couples uptake with phosphorylation of a variety of carbohydrates in prokaryotes. In this multienzyme complex, the enzyme II (EII), a carbohydrate-specific permease, is constituted of two cytoplasmic domains, IIA and IIB, and a transmembrane channel IIC domain. Among the five families of EIIs identified in Escherichia coli, the galactitol-specific transporter (II(gat)) belongs to the glucitol family and is structurally the least well-characterized. Here, we used nuclear magnetic resonance (NMR) spectroscopy to solve the three-dimensional structure of the IIB subunit (GatB). GatB consists of a central four-stranded parallel beta-sheet flanked by alpha-helices on both sides; the active site cysteine of GatB is located at the beginning of an unstructured loop between beta1 and alpha1 that folds into a P-loop-like structure. This structural arrangement shows similarities with other IIB subunits but also with mammalian low molecular weight protein tyrosine phosphatases (LMW PTPase) and arsenate reductase (ArsC). An NMR titration was performed to identify the GatA-interacting residues.

PubMed: 16963640
DOI: 10.1110/ps.062337406

Experimental method

SOLUTION NMR