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J. Biol. Chem., Vol. 265, Issue 36, 22223-22227, 12, 1990
DM Clarke, TW Loo and DH MacLennan
Amino acids in three highly conserved segments of the Ca2(+)-ATPase.
Asp-Pro-Pro-Arg604, Thr-Gly-Asp627, Thr-Gly-Asp703 as well as Asp707, have
been proposed to participate in formation of the nucleotide binding site.
We have tested this hypothesis by investigating the properties of mutants
with alterations to amino acids within these segments. Most of the mutants
were found to be defective in Ca2+ transport function. The inactive mutants
could be separated into two classes on the basis of the kinetics of
phosphoenzyme intermediate formation and decomposition. One group,
Asp601----Asn, Pro603----Leu, Asp627----Glu, and Asp703----Asn, formed
phosphoenzyme intermediates with ATP in the presence of Ca2+ and with
inorganic phosphate only in the absence of Ca2+, indicating that both the
high affinity Ca2+ binding sites and the nucleotide binding sites were
intact. In each of these mutants, however, the ADP-sensitive phosphoenzyme
intermediate (E1P) decayed to the ADP-insensitive phosphoenzyme
intermediate very slowly, relative to the wild-type enzyme. Thus the
inability of these mutants to transport Ca2+ was accounted for by an
apparent block of the transport reaction at the E1P to E2P conformational
transition. Another group, Asp601----Glu, Pro603----Gly, Asp707----Glu, and
Asp707----Asn, did not form detectable phosphoenzyme intermediates from
either ATP or Pi. Although we have demonstrated an effect on Ca2+ transport
of mutations in each of the highly conserved regions predicted to be
involved in ATP binding, we cannot yet define their roles in ATP- dependent
Ca2+ transport.
Functional consequences of alterations to amino acids located in the nucleotide binding domain of the Ca2(+)-ATPase of sarcoplasmic reticulum
Banting and Best Department of Medical Research, Charles H. Best Institute, University of Toronto, Ontario, Canada.
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