1j1u: Difference between revisions

Revision as of 14:22, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1j1u.png

Template:STRUCTURE 1j1u

Crystal structure of archaeal tyrosyl-tRNA synthetase complexed with tRNA(Tyr) and L-tyrosineCrystal structure of archaeal tyrosyl-tRNA synthetase complexed with tRNA(Tyr) and L-tyrosine

Template:ABSTRACT PUBMED 12754495

About this StructureAbout this Structure

1J1U is a Single protein structure of sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for orthogonal tRNA specificities of tyrosyl-tRNA synthetases for genetic code expansion., Kobayashi T, Nureki O, Ishitani R, Yaremchuk A, Tukalo M, Cusack S, Sakamoto K, Yokoyama S, Nat Struct Biol. 2003 Jun;10(6):425-32. PMID:12754495

Page seeded by OCA on Tue Jul 1 14:22:26 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1j1u.gif|left|200px]]
+{{Seed}}
+[[Image:1j1u.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1j1u|  PDB=1j1u  |  SCENE=  }}
-'''Crystal structure of archaeal tyrosyl-tRNA synthetase complexed with tRNA(Tyr) and L-tyrosine'''
+===Crystal structure of archaeal tyrosyl-tRNA synthetase complexed with tRNA(Tyr) and L-tyrosine===
-==Overview==
+<!--
-The archaeal/eukaryotic tyrosyl-tRNA synthetase (TyrRS)-tRNA(Tyr) pairs do not cross-react with their bacterial counterparts. This 'orthogonal' condition is essential for using the archaeal pair to expand the bacterial genetic code. In this study, the structure of the Methanococcus jannaschii TyrRS-tRNA(Tyr)-L-tyrosine complex, solved at a resolution of 1.95 A, reveals that this archaeal TyrRS strictly recognizes the C1-G72 base pair, whereas the bacterial TyrRS recognizes the G1-C72 in a different manner using different residues. These diverse tRNA recognition modes form the basis for the orthogonality. The common tRNA(Tyr) identity determinants (the discriminator, A73 and the anticodon residues) are also recognized in manners different from those of the bacterial TyrRS. Based on this finding, we created a mutant TyrRS that aminoacylates the amber suppressor tRNA with C34 65 times more efficiently than does the wild-type enzyme.
+The line below this paragraph, {{ABSTRACT_PUBMED_12754495}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12754495 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12754495}}
 ==About this Structure==
@@ Line 37: / Line 41: @@
 [[Category: Structural genomic]]
 [[Category: Trna]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 20:42:06 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 14:22:26 2008''