2zim: Difference between revisions

Revision as of 13:12, 29 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:2zim.png

Template:STRUCTURE 2zim

Pyrrolysyl-tRNA synthetase bound to adenylated pyrrolysine and pyrophosphatePyrrolysyl-tRNA synthetase bound to adenylated pyrrolysine and pyrophosphate

Template:ABSTRACT PUBMED 17592110

About this StructureAbout this Structure

2ZIM is a Single protein structure of sequence from Methanosarcina mazei. Full crystallographic information is available from OCA.

ReferenceReference

Structure of pyrrolysyl-tRNA synthetase, an archaeal enzyme for genetic code innovation., Kavran JM, Gundllapalli S, O'Donoghue P, Englert M, Soll D, Steitz TA, Proc Natl Acad Sci U S A. 2007 Jul 3;104(27):11268-73. Epub 2007 Jun 25. PMID:17592110

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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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-'''Pyrrolysyl-tRNA synthetase bound to adenylated pyrrolysine and pyrophosphate'''
+===Pyrrolysyl-tRNA synthetase bound to adenylated pyrrolysine and pyrophosphate===
-==Overview==
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-Pyrrolysine (Pyl), the 22nd natural amino acid and genetically encoded by UAG, becomes attached to its cognate tRNA by pyrrolysyl-tRNA synthetase (PylRS). We have determined three crystal structures of the Methanosarcina mazei PylRS complexed with either AMP-PNP, Pyl-AMP plus pyrophosphate, or the Pyl analogue N-epsilon-[(cylopentyloxy)carbonyl]-L-lysine plus ATP. The structures reveal that PylRS utilizes a deep hydrophobic pocket for recognition of the Pyl side chain. A comparison of these structures with previously determined class II tRNA synthetase complexes illustrates that different substrate specificities derive from changes in a small number of residues that form the substrate side-chain-binding pocket. The knowledge of these structures allowed the placement of PylRS in the aminoacyl-tRNA synthetase (aaRS) tree as the last known synthetase that evolved for genetic code expansion, as well as the finding that Pyl arose before the last universal common ancestral state. The PylRS structure provides an excellent framework for designing new aaRSs with altered amino acid specificity.
+The line below this paragraph, {{ABSTRACT_PUBMED_17592110}}, adds the Publication Abstract to the page
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 [[Category: Protein biosynthesis]]
 [[Category: Trna synthetase bound to an adenylated intermediate]]
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