1v9h | pdb_00001v9h
Crystal structure of the RNase MC1 mutant Y101A in complex with 5'-UMP
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Overview
The ribonuclease MC1 (RNase MC1) from the seeds of the bitter gourd, belongs to the RNase T2 family. We evaluated the contribution of 11 amino, acids conserved in the RNase T2 family to protein folding of RNase MC1., Thermal unfolding experiments showed that substitution of Tyr(101), Phe(102), Ala(105), and Phe(190) resulted in a significant decrease in, themostability; the T(m) values were 47-58 degrees C compared to that for, the wild type (64 degrees C). Mutations of Pro(125), Gly(127), Gly(144), and Val(165) caused a moderate decrease in thermostability (T(m): 60-62, degrees C). In contrast, mutations of Asp(107) and Gly(173) did little, effect on thermostability. The contribution of Tyr(101), Phe(102), Pro(125), and Gly(127) to protein stability was further corroborated by, means of Gdn-HCl unfolding and protease digestions. Taken together, it, appeared that Tyr(101), Phe(102), Ala(105), Pro(125), Gly(127), Gly(144), Leu(162), Val(165), and Phe(190) conserved in the RNase T2 family play an, important role in the stability of the proteins.
About this Structure
1V9H is a Single protein structure of sequence from Momordica charantia with SO4 and U5P as ligands. Active as Ribonuclease T(2), with EC number 3.1.27.1 Full crystallographic information is available from OCA.
Reference
Amino acids conserved at the C-terminal half of the ribonuclease T2 family contribute to protein stability of the enzymes., Kimura K, Numata T, Kakuta Y, Kimura M, Biosci Biotechnol Biochem. 2004 Aug;68(8):1748-57. PMID:15322360
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