ABCMdb

PMID: 7545672

Ko YH, Pedersen PL
The first nucleotide binding fold of the cystic fibrosis transmembrane conductance regulator can function as an active ATPase.
J Biol Chem. 1995 Sep 22;270(38):22093-6., [PubMed]

Sentences

No. Mutations Sentence Comment

4 ABCC7 p.Lys464His ABCC7 p.Lys464Leu Significantly, the mutations K464H and K464L in the Walker A consensus motif of NBF1 markedly impair its catalytic capacity. Login to comment 42 ABCC7 p.Lys464His ABCC7 p.Lys464Leu K464H: 59-ACT GGA GCA GGC CAC ACT TCA CTT CTA-39 K464L: 59-ACT GGA GCA GGC CTG ACT TCA CTT CTA-39 The identity of the two base changes was confirmed by DNA sequencing (20). Login to comment 43 ABCC7 p.Lys464His ABCC7 p.Lys464Leu K464H: 5Ј-ACT GGA GCA GGC CAC ACT TCA CTT CTA-3Ј K464L: 5Ј-ACT GGA GCA GGC CTG ACT TCA CTT CTA-3Ј The identity of the two base changes was confirmed by DNA sequencing (20). Login to comment 112 ABCC7 p.Lys464His ABCC7 p.Lys464Leu B, comparison of the purity of wild type and mutant MBP-NBF1 proteins (K464H and K464L). Login to comment 113 ABCC7 p.Lys464His ABCC7 p.Lys464Leu B, comparison of the purity of wild type and mutant MBP-NBF1 proteins (K464H and K464L). Login to comment 114 ABCC7 p.Lys464His ABCC7 p.Lys464Leu C and D, the effect of the mutations K464H and K464L within NBF1 on the ATP hydrolytic activity of MBP-NBF1. Login to comment 115 ABCC7 p.Lys464His ABCC7 p.Lys464Leu C and D, the effect of the mutations K464H and K464L within NBF1 on the ATP hydrolytic activity of MBP-NBF1. Login to comment 124 ABCC7 p.Lys464His ABCC7 p.Lys464Leu Even more convincing are results presented in Fig. 4, C and D, where it is seen that the mutations, K464H and K464L, in the Walker A nucleotide binding motif (GX4GKT) of NBF1 reduce the ATP hydrolytic capacity of purified mutant MBP-NBF1 proteins by over 80%. Login to comment 125 ABCC7 p.Lys464His ABCC7 p.Lys464Leu Even more convincing are results presented in Fig. 4, C and D, where it is seen that the mutations, K464H and K464L, in the Walker A nucleotide binding motif (GX4GKT) of NBF1 reduce the ATP hydrolytic capacity of purified mutant MBP-NBF1 proteins by over 80%. Login to comment 132 ABCC7 p.Lys464His ABCC7 p.Lys464Leu The additional experimental results demonstrating that MBP alone has no catalytic capacity (Fig. 2C) and that mutations (K464H and K464L) within the Walker nucleotide binding motif GX4GKT markedly inhibit ATPase activity (Fig. 4, C and D) localize the catalytic site to NBF1. Login to comment 133 ABCC7 p.Lys464His ABCC7 p.Lys464Leu The additional experimental results demonstrating that MBP alone has no catalytic capacity (Fig. 2C) and that mutations (K464H and K464L) within the Walker nucleotide binding motif GX4GKT markedly inhibit ATPase activity (Fig. 4, C and D) localize the catalytic site to NBF1. Login to comment