1h3n

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(New page: 200px<br /> <applet load="1h3n" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h3n, resolution 2.00&Aring;" /> '''LEUCYL-TRNA SYNTHET...)
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==About this Structure==
==About this Structure==
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1H3N 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 ZN, SO4 and LEU as [[http://en.wikipedia.org/wiki/ligands ligands]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H3N OCA]].
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1H3N 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 ZN, SO4 and LEU as [[http://en.wikipedia.org/wiki/ligands ligands]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H3N OCA]].
==Reference==
==Reference==
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[[Category: class i aminoacyl-trna synthetase]]
[[Category: class i aminoacyl-trna synthetase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 19:20:51 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:30:06 2007''

Revision as of 10:25, 30 October 2007


1h3n, resolution 2.00Å

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LEUCYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH A SULPHAMOYL ANALOGUE OF LEUCYL-ADENYLATE

Overview

Leucyl-, isoleucyl- and valyl-tRNA synthetases are closely related large, monomeric class I synthetases. Each contains a homologous insertion domain, of approximately 200 residues, which is thought to permit them to, hydrolyse ('edit') cognate tRNA that has been mischarged with a chemically, similar but non-cognate amino acid. We describe the first crystal, structure of a leucyl-tRNA synthetase, from the hyperthermophile Thermus, thermophilus, at 2.0 A resolution. The overall architecture is similar to, that of isoleucyl-tRNA synthetase, except that the putative editing domain, is inserted at a different position in the primary structure. This feature, is unique to prokaryote-like leucyl-tRNA synthetases, as is the presence, of a novel additional flexibly inserted domain. Comparison of ... [(full description)]

About this Structure

1H3N is a [Single protein] structure of sequence from [Thermus thermophilus] with ZN, SO4 and LEU as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

The 2 A crystal structure of leucyl-tRNA synthetase and its complex with a leucyl-adenylate analogue., Cusack S, Yaremchuk A, Tukalo M, EMBO J. 2000 May 15;19(10):2351-61. PMID:10811626[[Category: atp + l-leucine + trna (leu) -> amp + ppi + l-leucyl-trna(leu)]]

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