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| - | [[Image:1det.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1det| PDB=1det | SCENE= }} | | {{STRUCTURE_1det| PDB=1det | SCENE= }} |
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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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| - | ==Overview==
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| - | 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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_8679590}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8679590 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_8679590}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Nuclease]] | | [[Category: Nuclease]] |
| | [[Category: Signal]] | | [[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 Mon Jun 30 22:54:57 2008'' |
Revision as of 19:54, 30 June 2008
Template:STRUCTURE 1det
RIBONUCLEASE T1 CARBOXYMETHYLATED AT GLU 58 IN COMPLEX WITH 2'GMP
Template:ABSTRACT PUBMED 8679590
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 Mon Jun 30 22:54:57 2008
