1h3n

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[[Image:1h3n.gif|left|200px]]
[[Image:1h3n.gif|left|200px]]
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{{Structure
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|PDB= 1h3n |SIZE=350|CAPTION= <scene name='initialview01'>1h3n</scene>, resolution 2.00&Aring;
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The line below this paragraph, containing "STRUCTURE_1h3n", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Lms+Binding+Site+For+Chain+A'>AC1</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=LEU:LEUCINE'>LEU</scene>, <scene name='pdbligand=LMS:[(2R,3S,4R,5R)-5-(6-AMINO-9H-PURIN-9-YL)-3,4-DIHYDROXYTETRAHYDRO-2-FURANYL]METHYL+SULFAMATE'>LMS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1h3n| PDB=1h3n | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h3n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h3n OCA], [http://www.ebi.ac.uk/pdbsum/1h3n PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h3n RCSB]</span>
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}}
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'''LEUCYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH A SULPHAMOYL ANALOGUE OF LEUCYL-ADENYLATE'''
'''LEUCYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH A SULPHAMOYL ANALOGUE OF LEUCYL-ADENYLATE'''
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[[Category: Tukalo, M.]]
[[Category: Tukalo, M.]]
[[Category: Yaremchuk, A.]]
[[Category: Yaremchuk, A.]]
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[[Category: atp + l-leucine + trna (leu) -> amp + ppi + l-leucyl-trna(leu)]]
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[[Category: Class i aminoacyl-trna synthetase]]
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[[Category: class i aminoacyl-trna synthetase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:23:31 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:57:00 2008''
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Revision as of 15:23, 2 May 2008

Template:STRUCTURE 1h3n

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 native enzyme and complexes with leucine and a leucyl- adenylate analogue shows that binding of the adenosine moiety of leucyl-adenylate causes significant conformational changes in the active site required for amino acid activation and tight binding of the adenylate. These changes are propagated to more distant regions of the enzyme, leading to a significantly more ordered structure ready for the subsequent aminoacylation and/or editing steps.

About this Structure

1H3N is a Single protein structure of sequence from Thermus thermophilus. 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 Page seeded by OCA on Fri May 2 18:23:31 2008

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