1low

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{{Seed}}
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{{STRUCTURE_1low| PDB=1low | SCENE= }}
{{STRUCTURE_1low| PDB=1low | SCENE= }}
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'''X-ray structure of the H40A mutant of Ribonuclease T1 complexed with 3'-guanosine monophosphate'''
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===X-ray structure of the H40A mutant of Ribonuclease T1 complexed with 3'-guanosine monophosphate===
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==Overview==
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Ribonucleases (RNases) catalyze the cleavage of the phosphodiester bond in RNA up to 10(15)-fold, as compared with the uncatalyzed reaction. High resolution crystal structures of these enzymes in complex with 3'-mononucleotide substrates demonstrate the accommodation of the nucleophilic 2'-OH group in a binding pocket comprising the catalytic base (glutamate or histidine) and a charged hydrogen bond donor (lysine or histidine). Ab initio quantum chemical calculations performed on such Michaelis complexes of the mammalian RNase A (EC ) and the microbial RNase T(1) (EC ) show negative charge build up on the 2'-oxygen upon substrate binding. The increased nucleophilicity results from stronger hydrogen bonding to the catalytic base, which is mediated by a hydrogen bond from the charged donor. This hitherto unrecognized catalytic dyad in ribonucleases constitutes a general mechanism for nucleophile activation in both enzymic and RNA-catalyzed phosphoryl transfer reactions.
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The line below this paragraph, {{ABSTRACT_PUBMED_12122018}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 12122018 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12122018}}
==About this Structure==
==About this Structure==
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[[Category: Nucleophile activation]]
[[Category: Nucleophile activation]]
[[Category: Rnase]]
[[Category: Rnase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:07:52 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 21:39:43 2008''

Revision as of 18:39, 2 July 2008

Image:1low.png

Template:STRUCTURE 1low

X-ray structure of the H40A mutant of Ribonuclease T1 complexed with 3'-guanosine monophosphate

Template:ABSTRACT PUBMED 12122018

About this Structure

1LOW is a Single protein structure of sequence from Aspergillus oryzae. Full crystallographic information is available from OCA.

Reference

A nucleophile activation dyad in ribonucleases. A combined X-ray crystallographic/ab initio quantum chemical study., Mignon P, Steyaert J, Loris R, Geerlings P, Loverix S, J Biol Chem. 2002 Sep 27;277(39):36770-4. Epub 2002 Jul 16. PMID:12122018

Page seeded by OCA on Wed Jul 2 21:39:43 2008

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