1loy
From Proteopedia
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[[Image:1loy.gif|left|200px]] | [[Image:1loy.gif|left|200px]] | ||
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'''X-ray structure of the H40A/E58A mutant of Ribonuclease T1 complexed with 3'-guanosine monophosphate''' | '''X-ray structure of the H40A/E58A mutant of Ribonuclease T1 complexed with 3'-guanosine monophosphate''' | ||
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12122018 12122018] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12122018 12122018] | ||
[[Category: Aspergillus oryzae]] | [[Category: Aspergillus oryzae]] | ||
| - | [[Category: Ribonuclease T(1)]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Geerlings, P.]] | [[Category: Geerlings, P.]] | ||
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[[Category: Mignon, P.]] | [[Category: Mignon, P.]] | ||
[[Category: Steyaert, J.]] | [[Category: Steyaert, J.]] | ||
| - | [[Category: | + | [[Category: Ab initio calculation]] |
| - | [[Category: | + | [[Category: Catalytic dyad]] |
| - | [[Category: | + | [[Category: Nucleophile activation]] |
| - | [[Category: | + | [[Category: Rnase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:07:59 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 21:08, 2 May 2008
X-ray structure of the H40A/E58A mutant of Ribonuclease T1 complexed with 3'-guanosine monophosphate
Overview
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.
About this Structure
1LOY 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 Sat May 3 00:07:59 2008
