1det
From Proteopedia
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'''RIBONUCLEASE T1 CARBOXYMETHYLATED AT GLU 58 IN COMPLEX WITH 2'GMP''' | '''RIBONUCLEASE T1 CARBOXYMETHYLATED AT GLU 58 IN COMPLEX WITH 2'GMP''' | ||
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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:[http://www.ncbi.nlm.nih.gov/pubmed/8679590 8679590] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8679590 8679590] | ||
[[Category: Aspergillus oryzae]] | [[Category: Aspergillus oryzae]] | ||
| - | [[Category: Ribonuclease T(1)]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Ishikawa, K.]] | [[Category: Ishikawa, K.]] | ||
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[[Category: Takahashi, K.]] | [[Category: Takahashi, K.]] | ||
[[Category: Tanokura, M.]] | [[Category: Tanokura, M.]] | ||
| - | [[Category: | + | [[Category: Endonuclease]] |
| - | [[Category: | + | [[Category: Endoribonuclease]] |
| - | [[Category: | + | [[Category: Hydrolase]] |
| - | [[Category: | + | [[Category: Nuclease]] |
| - | [[Category: | + | [[Category: Signal]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:46:13 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 10:46, 2 May 2008
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 Page seeded by OCA on Fri May 2 13:46:13 2008
