| Choel Kim | ||
|
Structure of Anthranilate Phosphoribosyltransferase from the enterobacterium Erwinia Carotovora.
During my research, I solved the structure of anthranilate
phosphoribosyltranferase from the enterobacterium Erwinia carotovora. The
enzyme structure has a novel phosphoribosyltranferase fold, and
displays close homology to the structure of pyrimidine nucleoside
phosphorylase. The monomer of APRT consists of two domains, alpha
and alpha/beta. domain. The alpha domain is a small four-helix bundle,
sandwiched next to two additional helices. The alpha/beta-domain consists
of eight alpha-helices and one mixed sheet, 5 parallel strands and
two anti-parallel alpha strands. The active site of APRT is located at
the cleft between the alpha domain and the alpha/beta domain where the
trapped MnPPi complex is located. With APRT solved, the structures of
all the enzymes and regulatory proteins of tryptophan biosynthesis are
now known, the first biosynthetic pathway so delineated.
PUBLICATIONS (resulting from this training, and some recent ones)
Spraggon G, Kim C, Nguyen-Huu X, Yee MC, Yanofsky C, Mills SE. (2001) The
structures of anthranilate synthase of Serratia marcescens crystallized
in the presence of (i) its substrates, chorismate and glutamine, and a
product, glutamate, and (ii) its end-product inhibitor, L-tryptophan.
Proc Natl Acad Sci USA. 98:6021-6.
|
|
|||||