 |
PDBsum entry 3ogz
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
|
|
Title
|
|
Structural basis for the broad substrate range of the udp-Sugar pyrophosphorylase from leishmania major.
|
|
|
Authors
|
|
A.Dickmanns,
S.Damerow,
P.Neumann,
E.C.Schulz,
A.C.Lamerz,
F.H.Routier,
R.Ficner.
|
|
|
Ref.
|
|
J Mol Biol, 2011,
405,
461-478.
|
|
|
PubMed id
|
|
|
|
|
Note: In the PDB file this reference is
annotated as "TO BE PUBLISHED". The citation details given above have
been manually determined.
|
|
|
|
Abstract
|
|
|
Nucleotide sugars and the enzymes that are responsible for their synthesis are
indispensable for the production of complex carbohydrates and, thus, for
elaboration of a protective cellular coat for many organisms such as the
protozoan parasite Leishmania. These activated sugars are synthesized de novo or
derived from salvaged monosaccharides. In addition to UDP-glucose (UDP-Glc)
pyrophosphorylase, which catalyzes the formation of UDP-Glc from substrates UTP
and glucose-1-phosphate, Leishmania major and plants express a UDP-sugar
pyrophosphorylase (USP) that exhibits broad substrate specificity in vitro. The
enzyme, likely involved in monosaccharide salvage, preferentially generates
UDP-Glc and UDP-galactose, but it may also activate other hexose- or
pentose-1-phosphates such as galacturonic acid-1-phosphate or
arabinose-1-phosphate. In order to gain insight into structural features
governing the differences in substrate specificity, we determined the crystal
structure of the L. major USP in the APO-, UTP-, and UDP-sugar-bound
conformations. The overall tripartite structure of USP exhibits a significant
structural homology to other nucleotidyldiphosphate-glucose pyrophosphorylases.
The obtained USP structures reveal the structural rearrangements occurring
during the stepwise binding process of the substrates. Moreover, the different
product complexes explain the broad substrate specificity of USP, which is
enabled by structural changes in the sugar binding region of the active site.
|
|
|
|
|
|
|
