INTERACTION OF PYROPHOSPHATE MOIETIES WITH ALPHA-HELIXES IN DINUCLEOTIDE BINDING-PROTEINS
INTERACTION OF PYROPHOSPHATE MOIETIES WITH ALPHA-HELIXES IN DINUCLEOTIDE BINDING-PROTEINS
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DOI:
10.1021/bi00327a012
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发表时间:
1985-01-01
期刊:
影响因子:
2.9
通讯作者:
HOL, WGJ
中科院分区:
文献类型:
--
作者:
WIERENGA, RK;DEMAEYER, MCH;HOL, WGJ
The binding of dinucleotide pyrophosphate moieties to those proteins where helixes play an important role in the binding was studied. The 3-dimensional structures and amino acid sequences of 6 proteins interacting with 3 different dinucleotides were available. As glutathione reductase binds 2 dinucleotides, 7 enzyme-dinucleotide complxes were studied. In all these complexes the pyrophosphate moiety is located near the N-terminus of at least 1 .alpha.-helix, the dinucleotide binding helix. In dihydrofolate reductase 2 helixes interact with the pyrophosphate of NADP. Only 2 common characteristics of all complxes are observed: the occurrence of a glycine at the N-terminus of the helix and the favorable interaction of the .alpha.-helix dipole with the negatively charged pyrophosphate moiety. In virtually every other respect, the dinucleotide binding by dihydrofolate reductase differs from the mode of binding by the 5 other proteins. The helixes of these 5 proteins were grouped together as category I dinucleotide binding helixes. The 6 category I helixes form part of a compact .beta..alpha..beta. unit of highly similar structure and very dissimilar sequences. A characteristic fingerprint for the sequence of this unit can be deduced. Only the ADP moieties of the dinucleotides occupy very similar positions with respect to these compact .beta..alpha..beta. units. An appropriate name for these units would be ADP binding .beta..alpha..beta. folds.