ABCC1 p.Thr140Met
| Predicted by SNAP2: | A: N (66%), C: N (93%), D: N (61%), E: D (53%), F: N (78%), G: N (72%), H: N (57%), I: N (93%), K: D (63%), L: N (93%), M: N (87%), N: N (78%), P: N (61%), Q: N (66%), R: D (59%), S: N (82%), V: N (93%), W: D (53%), Y: N (82%), |
| Predicted by PROVEAN: | A: N, C: N, D: N, E: N, F: N, G: D, H: N, I: N, K: N, L: N, M: N, N: N, P: N, Q: N, R: N, S: N, V: N, W: N, Y: N, |
[switch to compact view]
Comments [show]
None has been submitted yet.
[hide] Eukaryotic ribonucleases P/MRP: the crystal struct... EMBO J. 2010 Feb 17;29(4):761-9. doi: 10.1038/emboj.2009.396. Epub 2010 Jan 14. Perederina A, Esakova O, Quan C, Khanova E, Krasilnikov AS
Eukaryotic ribonucleases P/MRP: the crystal structure of the P3 domain.
EMBO J. 2010 Feb 17;29(4):761-9. doi: 10.1038/emboj.2009.396. Epub 2010 Jan 14., [PMID:20075859]
Abstract [show]
Ribonuclease (RNase) P is a site-specific endoribonuclease found in all kingdoms of life. Typical RNase P consists of a catalytic RNA component and a protein moiety. In the eukaryotes, the RNase P lineage has split into two, giving rise to a closely related enzyme, RNase MRP, which has similar components but has evolved to have different specificities. The eukaryotic RNases P/MRP have acquired an essential helix-loop-helix protein-binding RNA domain P3 that has an important function in eukaryotic enzymes and distinguishes them from bacterial and archaeal RNases P. Here, we present a crystal structure of the P3 RNA domain from Saccharomyces cerevisiae RNase MRP in a complex with RNase P/MRP proteins Pop6 and Pop7 solved to 2.7 A. The structure suggests similar structural organization of the P3 RNA domains in RNases P/MRP and possible functions of the P3 domains and proteins bound to them in the stabilization of the holoenzymes' structures as well as in interactions with substrates. It provides the first insight into the structural organization of the eukaryotic enzymes of the RNase P/MRP family.
Comments [show]
None has been submitted yet.
No. Sentence Comment
179 To provide additional reference points for the assignment of residues, nine mutants containing one additional methionine in each were produced: Pop6 mutants L115M, T140M and L141M; Pop7 mutants L24M, L52M, L78M, C80M, L100M and L136M.
X
ABCC1 p.Thr140Met 20075859:179:164
status: NEW181 During subsequent crystallization trials, the complexes containing the Pop6 mutant T140M, Pop7 mutants L78M and C80M failed to crystallize in conditions similar to the original crystallization conditions.
X
ABCC1 p.Thr140Met 20075859:181:83
status: NEW180 To provide additional reference points for the assignment of residues, nine mutants containing one additional methionine in each were produced: Pop6 mutants L115M, T140M and L141M; Pop7 mutants L24M, L52M, L78M, C80M, L100M and L136M.
X
ABCC1 p.Thr140Met 20075859:180:164
status: NEW182 During subsequent crystallization trials, the complexes containing the Pop6 mutant T140M, Pop7 mutants L78M and C80M failed to crystallize in conditions similar to the original crystallization conditions.
X
ABCC1 p.Thr140Met 20075859:182:83
status: NEW