TY - JOUR
T1 - Backbone 1H, 13C, 15N NMR assignments of the unliganded and substrate ternary complex forms of mevalonate diphosphate decarboxylase from Streptococcus pneumoniae
AU - Reuther, Guido
AU - Harris, Richard
AU - Girvin, Mark
AU - Leyh, Thomas S.
N1 - Funding Information:
Acknowledgments This work is supported by NIH grant AI 068989. Many of the NMR experiments were performed at the New York Structural Biology Center, which is a STAR center supported by the New York State Office of Science, Technology, and Academic Research. We also thank Dr. Sean Cahill from the Einstein NMR facility.
PY - 2011/4
Y1 - 2011/4
N2 - Mevalonate diphosphate decarboxylase (MDD) catalyzes the ATP-dependent decarboxylation of diphosphomevalonate (DPM) to produce isopentenyl diphosphate (IPP), the molecular "building block" for more than 25,000 distinct isoprenoids, including cholesterol, steroid hormones and terpenoids. Here, we present the first backbone assignment of Streptococcus pneumoniae MDD in the unliganded state and in a ternary complex with DPM and AMPPCP - a nucleotide analogue unable to transfer the γ-phosphoryl group. The secondary chemical shifts for the unliganded form are in good agreement with the crystal structure of Streptococcus pyogenes (~70% sequence identity). The addition of substrate and nucleotide to the enzyme results in chemical shift changes of cross peaks that correspond to residues in the binding pocket.
AB - Mevalonate diphosphate decarboxylase (MDD) catalyzes the ATP-dependent decarboxylation of diphosphomevalonate (DPM) to produce isopentenyl diphosphate (IPP), the molecular "building block" for more than 25,000 distinct isoprenoids, including cholesterol, steroid hormones and terpenoids. Here, we present the first backbone assignment of Streptococcus pneumoniae MDD in the unliganded state and in a ternary complex with DPM and AMPPCP - a nucleotide analogue unable to transfer the γ-phosphoryl group. The secondary chemical shifts for the unliganded form are in good agreement with the crystal structure of Streptococcus pyogenes (~70% sequence identity). The addition of substrate and nucleotide to the enzyme results in chemical shift changes of cross peaks that correspond to residues in the binding pocket.
KW - Mevalonate diphosphate decarboxylase (MDD)
KW - NMR resonance assignments
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U2 - 10.1007/s12104-010-9255-4
DO - 10.1007/s12104-010-9255-4
M3 - Article
C2 - 20737255
AN - SCOPUS:79952448915
SN - 1874-2718
VL - 5
SP - 11
EP - 14
JO - Biomolecular NMR Assignments
JF - Biomolecular NMR Assignments
IS - 1
ER -