1v9h

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[[Image:1v9h.jpg|left|200px]]<br /><applet load="1v9h" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1v9h.jpg|left|200px]]
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caption="1v9h, resolution 2.00&Aring;" />
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'''Crystal structure of the RNase MC1 mutant Y101A in complex with 5'-UMP'''<br />
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{{Structure
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|PDB= 1v9h |SIZE=350|CAPTION= <scene name='initialview01'>1v9h</scene>, resolution 2.00&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=U5P:URIDINE-5'-MONOPHOSPHATE'>U5P</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Ribonuclease_T(2) Ribonuclease T(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.1 3.1.27.1]
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|GENE=
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}}
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'''Crystal structure of the RNase MC1 mutant Y101A in complex with 5'-UMP'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1V9H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Momordica_charantia Momordica charantia] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=U5P:'>U5P</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_T(2) Ribonuclease T(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.1 3.1.27.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V9H OCA].
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1V9H is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Momordica_charantia Momordica charantia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V9H OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15322360 15322360]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15322360 15322360]
[[Category: Momordica charantia]]
[[Category: Momordica charantia]]
[[Category: Ribonuclease T(2)]]
[[Category: Ribonuclease T(2)]]
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[[Category: rna]]
[[Category: rna]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:32:55 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:42:35 2008''

Revision as of 12:42, 20 March 2008

Image:1v9h.jpg


PDB ID 1v9h

Drag the structure with the mouse to rotate
, resolution 2.00Å
Ligands: and
Activity: Ribonuclease T(2), with EC number 3.1.27.1
Coordinates: save as pdb, mmCIF, xml



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


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. 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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