This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1nj2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1nj2.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1nj2.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1nj2| PDB=1nj2 | SCENE= }}
{{STRUCTURE_1nj2| PDB=1nj2 | SCENE= }}
-
'''Crystal structure of Prolyl-tRNA Synthetase from Methanothermobacter thermautotrophicus'''
+
===Crystal structure of Prolyl-tRNA Synthetase from Methanothermobacter thermautotrophicus===
-
==Overview==
+
<!--
-
Cysteinyl-tRNA synthetase is an essential enzyme required for protein synthesis. Genes encoding this protein have not been identified in Methanocaldococcus jannaschii, Methanothermobacter thermautotrophicus, or Methanopyrus kandleri. It has previously been proposed that the prolyl-tRNA synthetase (ProRS) enzymes in these organisms recognize either proline or cysteine and can aminoacylate their cognate tRNAs through a dual-specificity mechanism. We report five crystal structures at resolutions between 2.6 and 3.2 A: apo M. jannaschii ProRS, and M. thermautotrophicus ProRS in apo form and in complex with cysteinyl-sulfamoyl-, prolyl-sulfamoyl-, and alanyl-sulfamoyl-adenylates. These aminoacyl-adenylate analogues bind to a single active-site pocket and induce an identical set of conformational changes in loops around the active site when compared with the ligand-free conformation of ProRS. The cysteinyl- and prolyl-adenylate analogues have similar, nanomolar affinities for M. thermautotrophicus ProRS. Homology modeling of tRNA onto these adenylate complexes places the 3'-OH of A76 in an appropriate position for the transfer of any of the three amino acids to tRNA. Thus, these structures explain recent biochemical experiments showing that M. jannaschii ProRS misacylates tRNA(Pro) with cysteine, and argue against the proposal that these archaeal ProRS enzymes possess the dual capacity to aminoacylate both tRNA(Pro) and tRNA(Cys) with their cognate amino acids.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12578991}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12578991 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12578991}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Wang, J.]]
[[Category: Wang, J.]]
[[Category: Class-ii trna synthetase]]
[[Category: Class-ii trna synthetase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:35:34 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:02:04 2008''

Revision as of 10:02, 29 July 2008

Image:1nj2.png

Template:STRUCTURE 1nj2

Crystal structure of Prolyl-tRNA Synthetase from Methanothermobacter thermautotrophicus

Template:ABSTRACT PUBMED 12578991

About this Structure

1NJ2 is a Single protein structure of sequence from Methanothermobacter thermautotrophicus. Full crystallographic information is available from OCA.

Reference

The structural basis of cysteine aminoacylation of tRNAPro by prolyl-tRNA synthetases., Kamtekar S, Kennedy WD, Wang J, Stathopoulos C, Soll D, Steitz TA, Proc Natl Acad Sci U S A. 2003 Feb 18;100(4):1673-8. Epub 2003 Feb 10. PMID:12578991

Page seeded by OCA on Tue Jul 29 13:02:04 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1nj2"
Personal tools