1v9h

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

Structural highlights

1v9h is a 1 chain structure with sequence from Momordica charantia. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:SO4, U5P
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RNMC1_MOMCH Ribonuclease cleaving preferentially the 5'-side of uridine.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
1 reviews cite this structure
T2 Family ribonucleases: ancient enzymes with diverse roles.
Luhtala et al. (2010)
0 more
1 other articles
No citations found

See Also

References

  1. ↑ Suzuki A, Yao M, Tanaka I, Numata T, Kikukawa S, Yamasaki N, Kimura M. Crystal structures of the ribonuclease MC1 from bitter gourd seeds, complexed with 2'-UMP or 3'-UMP, reveal structural basis for uridine specificity. Biochem Biophys Res Commun. 2000 Aug 28;275(2):572-6. PMID:10964705 doi:10.1006/bbrc.2000.3318
  2. ↑ 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. 2004 Aug;68(8):1748-57. PMID:15322360

Contents


PDB ID 1v9h

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OCA

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