1h4v: Difference between revisions
New page: left|200px<br /> <applet load="1h4v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h4v, resolution 2.4Å" /> '''HISTIDYL-TRNA SYNTHE... |
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==About this Structure== | ==About this Structure== | ||
1H4V is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]] with SO4 as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.21 6.1.1.21]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H4V OCA]]. | 1H4V is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]] with SO4 as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Histidine--tRNA_ligase Histidine--tRNA ligase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.21 6.1.1.21]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H4V OCA]]. | ||
==Reference== | ==Reference== | ||
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11399074 11399074] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11399074 11399074] | ||
[[Category: Histidine--tRNA ligase]] | |||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermus thermophilus]] | [[Category: Thermus thermophilus]] | ||
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[[Category: class iia aminoacyl-trna synthetase]] | [[Category: class iia aminoacyl-trna synthetase]] | ||
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Revision as of 13:37, 30 October 2007
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HISTIDYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS (LIGAND FREE)
OverviewOverview
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 ... [(full description)]
About this StructureAbout this Structure
1H4V is a [Single protein] structure of sequence from [Thermus thermophilus] with SO4 as [ligand]. Active as [Histidine--tRNA ligase], with EC number [6.1.1.21]. Structure known Active Site: AC1. 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 [[Category: atp + l-histidine trna(his)-> amp + ppi + l-histidyl-trna(his)]]
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