1994
DOI: 10.1016/s0021-9258(17)41934-x
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Functionally important residues at a subunit interface site in the RecA protein from Escherichia coli.

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Cited by 42 publications
(7 citation statements)
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“…Biochemical and biophysical experiments conducted over the past two decades have helped generate a broad outline of the molecular events that constitute the RecA catalytic cycle. ,, The interaction of the carboxamide group of Gln194/196 with ATP leads to a conformational change in DNA binding loop L2, causing it to acquire an extended β-sheet conformation . The information is then transmitted along the peptide backbone of L2, to α-helix 8 downstream of L2, resulting in the insertion of a conserved phenylalanine (Phe217/219), into a hydrophobic pocket in the neighboring RecA molecule .…”
Section: Discussionmentioning
confidence: 99%
“…Biochemical and biophysical experiments conducted over the past two decades have helped generate a broad outline of the molecular events that constitute the RecA catalytic cycle. ,, The interaction of the carboxamide group of Gln194/196 with ATP leads to a conformational change in DNA binding loop L2, causing it to acquire an extended β-sheet conformation . The information is then transmitted along the peptide backbone of L2, to α-helix 8 downstream of L2, resulting in the insertion of a conserved phenylalanine (Phe217/219), into a hydrophobic pocket in the neighboring RecA molecule .…”
Section: Discussionmentioning
confidence: 99%
“…While the mutational stringency at K216 and R222 can be rationalized in terms of the contacts observed in the crystal structure, there appear to be no structural constraints that explain the stringency at F217 (6). However, several hydrophobic residues are seen clustered within a pocket in the neighboring subunit and may serve to stabilize a crosssubunit interaction with F217.…”
mentioning
confidence: 95%
“…In an effort to identify important determinants of the oligomeric structure of RecA, we previously introduced a number of mutations into one area of the protein (6) which is seen in the crystal structure (7) to contain a variety of intersubunit contacts. The sequence spanning residues 213-222 contains five amino acids (N213, K216, F217, Y218, and R222) whose side chains extend across the interface and contact positions in the neighboring subunit (6,7).…”
mentioning
confidence: 99%
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