1det
From Proteopedia
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|PDB= 1det |SIZE=350|CAPTION= <scene name='initialview01'>1det</scene>, resolution 1.8Å | |PDB= 1det |SIZE=350|CAPTION= <scene name='initialview01'>1det</scene>, resolution 1.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=2GP:GUANOSINE-2'-MONOPHOSPHATE'>2GP</scene>, <scene name='pdbligand=CGA:CARBOXYMETHYLATED+GLUTAMIC+ACID'>CGA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1det FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1det OCA], [http://www.ebi.ac.uk/pdbsum/1det PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1det RCSB]</span> | ||
}} | }} | ||
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[[Category: Takahashi, K.]] | [[Category: Takahashi, K.]] | ||
[[Category: Tanokura, M.]] | [[Category: Tanokura, M.]] | ||
| - | [[Category: 2GP]] | ||
| - | [[Category: NA]] | ||
[[Category: endonuclease]] | [[Category: endonuclease]] | ||
[[Category: endoribonuclease]] | [[Category: endoribonuclease]] | ||
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[[Category: signal]] | [[Category: signal]] | ||
| - | ''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 19:40:12 2008'' |
Revision as of 16:40, 30 March 2008
| |||||||
| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Activity: | Ribonuclease T(1), with EC number 3.1.27.3 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
RIBONUCLEASE T1 CARBOXYMETHYLATED AT GLU 58 IN COMPLEX WITH 2'GMP
Overview
The carboxymethylation of RNase T1 at the gamma-carboxyl group of Glu58 leads to a complete loss of the enzymatic activity while it retains substrate-binding ability. Accompanying the carboxymethylation, RNase T1 undergoes a remarkable thermal stabilization of 9 degrees C in the melting temperature (Tm). In order to clarify the inactivation and stabilization mechanisms of RNase T1 by carboxymethylation, the crystal structure of carboxymethylated RNase T1 (CM-RNase T1) complexed with 2'-GMP was determined at 1.8 A resolution. The structure, including 79 water molecules and two Na+, was refined to an R factor of 0.194 with 10 354 reflections > 1 sigma (F). The carboxyl group of CM-Glu58, which locates in the active site, occupies almost the same position as the phosphate group of 2'-GMP in the crystal structure of intact RNase T1.2'-GMP complex. Therefore, the phosphate group of 2'-GMP cannot locate in the active site but protrudes toward the solvent. This forces 2'-GMP to adopt an anti form, which contrasts with the syn form in the crystal of the intact RNase T1.2'-GMP complex. The inaccessibility of the phosphate group to the active site can account for the lack of the enzymatic activity in CM-RNase T1. One of the carboxyl oxygen atoms of CM-Glu58 forms two hydrogen bonds with the side-chains of Tyr38 and His40. These hydrogen bonds are considered to mainly contribute to the higher thermal stability of CM-RNase T1. Another carboxyl oxygen atoms of CM-Glu58 is situated nearby His40 and Arg77. This may provide additional electrostatic stabilization.
About this Structure
1DET is a Single protein structure of sequence from Aspergillus oryzae. Full crystallographic information is available from OCA.
Reference
Crystal structure of ribonuclease T1 carboxymethylated at Glu58 in complex with 2'-GMP., Ishikawa K, Suzuki E, Tanokura M, Takahashi K, Biochemistry. 1996 Jun 25;35(25):8329-34. PMID:8679590
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