We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1det

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1det.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1det.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1det| PDB=1det | SCENE= }}
{{STRUCTURE_1det| PDB=1det | SCENE= }}
-
'''RIBONUCLEASE T1 CARBOXYMETHYLATED AT GLU 58 IN COMPLEX WITH 2'GMP'''
+
===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 &gt; 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.
 +
-->
 +
{{ABSTRACT_PUBMED_8679590}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[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

Image:1det.png

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1det"
Personal tools