1h4v: Difference between revisions

Revision as of 06:37, 1 July 2008

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File:1h4v.png

Template:STRUCTURE 1h4v

HISTIDYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS (LIGAND FREE)HISTIDYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS (LIGAND FREE)

Template:ABSTRACT PUBMED 11399074

About this StructureAbout this Structure

1H4V is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

ReferenceReference

A succession of substrate induced conformational changes ensures the amino acid specificity of Thermus thermophilus prolyl-tRNA synthetase: comparison with histidyl-tRNA synthetase., Yaremchuk A, Tukalo M, Grotli M, Cusack S, J Mol Biol. 2001 Jun 15;309(4):989-1002. PMID:11399074

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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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 {{STRUCTURE_1h4v|  PDB=1h4v  |  SCENE=  }}
-'''HISTIDYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS (LIGAND FREE)'''
+===HISTIDYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS (LIGAND FREE)===
-==Overview==
+<!--
-We describe the recognition by Thermus thermophilus prolyl-tRNA synthetase (ProRSTT) of proline, ATP and prolyl-adenylate and the sequential conformational changes occurring when the substrates bind and the activated intermediate is formed. Proline and ATP binding cause respectively conformational changes in the proline binding loop and motif 2 loop. However formation of the activated intermediate is necessary for the final conformational ordering of a ten residue peptide ("ordering loop") close to the active site which would appear to be essential for functional tRNA 3' end binding. These induced fit conformational changes ensure that the enzyme is highly specific for proline activation and aminoacylation. We also present new structures of apo and AMP bound histidyl-tRNA synthetase (HisRS) from T. thermophilus which we compare to our previous structures of the histidine and histidyl-adenylate bound enzyme. Qualitatively, similar results to those observed with T. thermophilus prolyl-tRNA synthetase are found. However histidine binding is sufficient to induce the co-operative ordering of the topologically equivalent histidine binding loop and ordering loop. These two examples contrast with most other class II aminoacyl-tRNA synthetases whose pocket for the cognate amino acid side-chain is largely preformed. T. thermophilus prolyl-tRNA synthetase appears to be the second class II aminoacyl-tRNA synthetase, after HisRS, to use a positively charged amino acid instead of a divalent cation to catalyse the amino acid activation reaction.
+The line below this paragraph, {{ABSTRACT_PUBMED_11399074}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11399074 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11399074}}
 ==About this Structure==
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 [[Category: Yaremchuk, A.]]
 [[Category: Class iia aminoacyl-trna synthetase]]
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