| |
|
|
|
|
 |
| |
|
|
The NYSBC is the nation’s premier center for structural biology with unrivaled facilities for
Nuclear Magnetic Resonance Spectroscopy (NMR), Cryoelectron Microscopy
(CEM), and X-Ray Crystallography. NYSBC’s research facilities include
state-of-the-art instrumentation for analyzing proteins and other
molecules that trigger diseases, such as bacterial and viral
infections; disease and neurodegeneration; and trauma. The NYSBC is
located at 133rd Street and Convent Avenue in Manhattan.
|
|
News |
|
April 6, 2011
"Saccharides have a central role in the nutrition of all
living organisms. Whereas several saccharide uptake systems
are shared between the different phylogenetic kingdoms, the
phosphoenolpyruvate-dependent phosphotransferase system
exists almost exclusively in bacteria. This multi-component
system includes an integral membrane protein EIIC that
transports saccharides and assists in their
phosphorylation. Here we present the crystal structure
of an EIIC from Bacillus cereus that transports
diacetylchitobiose. The EIIC is a homodimer, with an
expansive interface formed between the amino-terminal halves
of the two protomers. The carboxy-terminal half of each
protomer has a large binding pocket that contains a
diacetylchitobiose, which is occluded from both sides of the
membrane with its site of phosphorylation near the conserved
His 250 and Glu 334 residues. The structure shows the
architecture of this important class of transporters,
identifies the determinants of substrate binding and
phosphorylation, and provides a framework for
understanding the mechanism of sugar translocation." -
Nature, April 6, 2011.
This crystal structure
was solved by
NYCOMPS researchers. See the full publication in Nature online
in April 2011.
click for more |
|
| |
|
|
|
|
|
|
| Copyright© 2000-2010 NYSBC • All rights reserved • Best viewed with IE(1024X768) • User Policy |
|
|
|
