| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-91 |
Sentence |
denotes |
Interaction of ATP binding sites in the ArsA ATPase, the catalytic subunit of the Ars pump. |
| T2 |
92-231 |
Sentence |
denotes |
The ArsA ATPase is the catalytic subunit of the Ars pump that catalyzes arsenical extrusion in Escherichia coli, thus providing resistance. |
| T3 |
232-329 |
Sentence |
denotes |
The active form of ArsA is a homodimer with four nucleotide binding sites, two from each monomer. |
| T4 |
330-492 |
Sentence |
denotes |
The codons for Gly-15 in the N-terminal consensus nucleotide binding sequence and Gly-334 in the C-terminal sequence were individually mutated to cysteine codons. |
| T5 |
493-679 |
Sentence |
denotes |
Cells expressing an arsAG334C mutation retained arsenite resistance, while an arsAG15C mutation resulted in substantial reductions in arsenite resistance, transport, and ATPase activity. |
| T6 |
680-791 |
Sentence |
denotes |
Selection for suppression of the G15C mutation that restored arsenite resistance yielded an A344V substitution. |
| T7 |
792-866 |
Sentence |
denotes |
Ala-344 is located adjacent to the C-terminal nucleotide binding sequence. |
| T8 |
867-1023 |
Sentence |
denotes |
The second site mutation did not suppress the loss of resistance resulting from G18D, G20S, or T22I substitutions in the N-terminal nucleotide binding site. |
| T9 |
1024-1098 |
Sentence |
denotes |
Cells expressing the G15C/A344V double mutant regained arsenite extrusion. |
| T10 |
1099-1239 |
Sentence |
denotes |
These results suggest a spatial proximity of Gly-15 and Ala-344 and support a model for interaction of the nucleotide binding sites in ArsA. |
| T1 |
0-91 |
Sentence |
denotes |
Interaction of ATP binding sites in the ArsA ATPase, the catalytic subunit of the Ars pump. |
| T2 |
92-231 |
Sentence |
denotes |
The ArsA ATPase is the catalytic subunit of the Ars pump that catalyzes arsenical extrusion in Escherichia coli, thus providing resistance. |
| T3 |
232-329 |
Sentence |
denotes |
The active form of ArsA is a homodimer with four nucleotide binding sites, two from each monomer. |
| T4 |
330-492 |
Sentence |
denotes |
The codons for Gly-15 in the N-terminal consensus nucleotide binding sequence and Gly-334 in the C-terminal sequence were individually mutated to cysteine codons. |
| T5 |
493-679 |
Sentence |
denotes |
Cells expressing an arsAG334C mutation retained arsenite resistance, while an arsAG15C mutation resulted in substantial reductions in arsenite resistance, transport, and ATPase activity. |
| T6 |
680-791 |
Sentence |
denotes |
Selection for suppression of the G15C mutation that restored arsenite resistance yielded an A344V substitution. |
| T7 |
792-866 |
Sentence |
denotes |
Ala-344 is located adjacent to the C-terminal nucleotide binding sequence. |
| T8 |
867-1023 |
Sentence |
denotes |
The second site mutation did not suppress the loss of resistance resulting from G18D, G20S, or T22I substitutions in the N-terminal nucleotide binding site. |
| T9 |
1024-1098 |
Sentence |
denotes |
Cells expressing the G15C/A344V double mutant regained arsenite extrusion. |
| T10 |
1099-1239 |
Sentence |
denotes |
These results suggest a spatial proximity of Gly-15 and Ala-344 and support a model for interaction of the nucleotide binding sites in ArsA. |
