1loy
From Proteopedia
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|PDB= 1loy |SIZE=350|CAPTION= <scene name='initialview01'>1loy</scene>, resolution 1.55Å | |PDB= 1loy |SIZE=350|CAPTION= <scene name='initialview01'>1loy</scene>, resolution 1.55Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=3GP:GUANOSINE-3'-MONOPHOSPHATE'>3GP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1rga|1RGA]], [[1rls|1RLS]], [[1lov|1LOV]], [[1low|1LOW]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1loy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1loy OCA], [http://www.ebi.ac.uk/pdbsum/1loy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1loy RCSB]</span> | ||
}} | }} | ||
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[[Category: Mignon, P.]] | [[Category: Mignon, P.]] | ||
[[Category: Steyaert, J.]] | [[Category: Steyaert, J.]] | ||
| - | [[Category: 3GP]] | ||
| - | [[Category: CA]] | ||
[[Category: ab initio calculation]] | [[Category: ab initio calculation]] | ||
[[Category: catalytic dyad]] | [[Category: catalytic dyad]] | ||
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[[Category: rnase]] | [[Category: rnase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:05:31 2008'' |
Revision as of 19:05, 30 March 2008
| |||||||
| , resolution 1.55Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Ribonuclease T(1), with EC number 3.1.27.3 | ||||||
| Related: | 1RGA, 1RLS, 1LOV, 1LOW
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Sun Mar 30 22:05:31 2008
