1riq: Difference between revisions

Revision as of 19:58, 27 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:1riq.png

Template:STRUCTURE 1riq

The crystal structure of the catalytic fragment of the alanyl-tRNA synthetaseThe crystal structure of the catalytic fragment of the alanyl-tRNA synthetase

Template:ABSTRACT PUBMED 15053876

About this StructureAbout this Structure

1RIQ is a Single protein structure of sequence from Aquifex aeolicus. Full crystallographic information is available from OCA.

ReferenceReference

Alanyl-tRNA synthetase crystal structure and design for acceptor-stem recognition., Swairjo MA, Otero FJ, Yang XL, Lovato MA, Skene RJ, McRee DE, Ribas de Pouplana L, Schimmel P, Mol Cell. 2004 Mar 26;13(6):829-41. PMID:15053876

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

OCA

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-'''The crystal structure of the catalytic fragment of the alanyl-tRNA synthetase'''
+===The crystal structure of the catalytic fragment of the alanyl-tRNA synthetase===
-==Overview==
+<!--
-Early work on aminoacylation of alanine-specific tRNA (tRNA(Ala)) by alanyl-tRNA synthetase (AlaRS) gave rise to the concept of an early "second genetic code" imbedded in the acceptor stems of tRNAs. A single conserved and position-specific G:U base pair in the tRNA acceptor stem is the key identity determinant. Further understanding has been limited due to lack of a crystal structure of the enzyme. We determined a 2.14 A crystal structure of the 453 amino acid catalytic fragment of Aquifex aeolicus AlaRS. It contains the catalytic domain characteristic of class II synthetases, a helical domain with a hairpin motif critical for acceptor-stem recognition, and a C-terminal domain of a mixed alpha/beta fold. Docking of tRNA(Ala) on AlaRS shows critical contacts with the three domains, consistent with previous mutagenesis and functional data. It also suggests conformational flexibility within the C domain, which might allow for the positional variation of the key G:U base pair seen in some tRNA(Ala)s.
+The line below this paragraph, {{ABSTRACT_PUBMED_15053876}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15053876 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15053876}}
 ==About this Structure==
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 [[Category: Class ii aminoacyl-trna synthetase]]
 [[Category: Helix-loop-helix motif]]
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