1V9H

Crystal structure of the RNase MC1 mutant Y101A in complex with 5'-UMP

Summary for 1V9H

• Entry DOI: 10.2210/pdb1v9h/pdb
• Descriptor: Ribonuclease MC, SULFATE ION, URIDINE-5'-MONOPHOSPHATE, ... (4 entities in total)
• Functional Keywords: hydolase, nucleic acid, rna, hydrolase
• Biological source: Momordica charantia (balsam pear)
• Total number of polymer chains: 1
• Total formula weight: 22540.07

Authors

Kimura, K.,Numata, T.,Kakuta, Y.,Kimura, M. (deposition date: 2004-01-26, release date: 2004-10-05, Last modification date: 2024-10-16)

Primary citation

Kimura, K.,Numata, T.,Kakuta, Y.,Kimura, M.
Amino acids conserved at the C-terminal half of the ribonuclease t2 family contribute to protein stability of the enzymes
Biosci.Biotechnol.Biochem., 68:1748-1757, 2004

PubMed Abstract: 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.

PubMed: 15322360
DOI: 10.1271/bbb.68.1748

Experimental method

X-RAY DIFFRACTION (2 Å)