1low: Difference between revisions
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[[Image:1low.gif|left|200px]] | [[Image:1low.gif|left|200px]] | ||
'''X-ray structure of the H40A mutant of Ribonuclease T1 complexed with 3'-guanosine monophosphate''' | {{Structure | ||
|PDB= 1low |SIZE=350|CAPTION= <scene name='initialview01'>1low</scene>, resolution 1.9Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=3GP:GUANOSINE-3'-MONOPHOSPHATE'>3GP</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Ribonuclease_T(1) Ribonuclease T(1)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.3 3.1.27.3] | |||
|GENE= | |||
}} | |||
'''X-ray structure of the H40A mutant of Ribonuclease T1 complexed with 3'-guanosine monophosphate''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1LOW is a [ | 1LOW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_oryzae Aspergillus oryzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LOW OCA]. | ||
==Reference== | ==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:[http:// | 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: Ribonuclease T(1)]] | ||
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[[Category: 3GP]] | [[Category: 3GP]] | ||
[[Category: CA]] | [[Category: CA]] | ||
[[Category: ab initio | [[Category: ab initio calculation]] | ||
[[Category: catalytic dyad]] | [[Category: catalytic dyad]] | ||
[[Category: nucleophile activation]] | [[Category: nucleophile activation]] | ||
[[Category: rnase]] | [[Category: rnase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:33:23 2008'' | ||
Revision as of 10:33, 20 March 2008
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| 1low, resolution 1.9Å | |||||||||||||
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| Ligands: | CA and 3GP | ||||||||||||
| Activity: | Ribonuclease T(1), with EC number 3.1.27.3 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
X-ray structure of the H40A 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
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
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