2bir
From Proteopedia
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|PDB= 2bir |SIZE=350|CAPTION= <scene name='initialview01'>2bir</scene>, resolution 2.30Å | |PDB= 2bir |SIZE=350|CAPTION= <scene name='initialview01'>2bir</scene>, resolution 2.30Å | ||
|SITE= <scene name='pdbsite=S1:Catalytic+Site'>S1</scene> | |SITE= <scene name='pdbsite=S1:Catalytic+Site'>S1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=2GP:GUANOSINE-2'-MONOPHOSPHATE'>2GP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bir FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bir OCA], [http://www.ebi.ac.uk/pdbsum/2bir PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bir RCSB]</span> | ||
}} | }} | ||
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[[Category: Loverix, S.]] | [[Category: Loverix, S.]] | ||
[[Category: Steyaert, J.]] | [[Category: Steyaert, J.]] | ||
| - | [[Category: 2GP]] | ||
| - | [[Category: CA]] | ||
[[Category: endonuclease]] | [[Category: endonuclease]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
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[[Category: signal]] | [[Category: signal]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:07:03 2008'' |
Revision as of 23:07, 30 March 2008
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| , resolution 2.30Å | |||||||
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| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ADDITIVITY OF SUBSTRATE BINDING IN RIBONUCLEASE T1 (Y42A MUTANT)
Overview
It has been established that Tyr-42, Tyr-45, and Glu-46 take part in a structural motif that renders guanine specificity to ribonuclease T1. We report on the impact of Tyr-42, Tyr-45, and Glu-46 substitutions on the guanine specificity of RNase T1. The Y42A and E46A mutations profoundly affect substrate binding. No such effect is observed for Y45A RNase T1. From the kinetics of the Y42A/Y45A and Y42A/E46A double mutants, we conclude that these pairs of residues contribute to guanine specificity in a mutually independent way. From our results, it appears that the energetic contribution of aromatic face-to-face stacking interactions may be significant if polycyclic molecules, such as guanine, are involved.
About this Structure
2BIR is a Single protein structure of sequence from Aspergillus oryzae. Full crystallographic information is available from OCA.
Reference
Additivity of protein-guanine interactions in ribonuclease T1., Loverix S, Doumen J, Steyaert J, J Biol Chem. 1997 Apr 11;272(15):9635-9. PMID:9092491
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