1obc

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[[Image:1obc.gif|left|200px]]<br /><applet load="1obc" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1obc.gif|left|200px]]
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caption="1obc, resolution 2.10&Aring;" />
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'''LEUCYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH A POST-TRANSFER EDITING SUBSTRATE ANALOGUE'''<br />
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{{Structure
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|PDB= 1obc |SIZE=350|CAPTION= <scene name='initialview01'>1obc</scene>, resolution 2.10&Aring;
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|SITE= <scene name='pdbsite=AC1:Lms+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=LEU:LEUCINE'>LEU</scene> and <scene name='pdbligand=LMS:[(2R,3S,4R,5R)-5-(6-AMINO-9H-PURIN-9-YL)-3,4-DIHYDROXYTETRAHYDRO-2-FURANYL]METHYL SULFAMATE'>LMS</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''LEUCYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH A POST-TRANSFER EDITING SUBSTRATE ANALOGUE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1OBC 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 <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=LEU:'>LEU</scene> and <scene name='pdbligand=LMS:'>LMS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Lms+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OBC OCA].
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1OBC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OBC OCA].
==Reference==
==Reference==
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Structural and mechanistic basis of pre- and posttransfer editing by leucyl-tRNA synthetase., Lincecum TL Jr, Tukalo M, Yaremchuk A, Mursinna RS, Williams AM, Sproat BS, Van Den Eynde W, Link A, Van Calenbergh S, Grotli M, Martinis SA, Cusack S, Mol Cell. 2003 Apr;11(4):951-63. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12718881 12718881]
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Structural and mechanistic basis of pre- and posttransfer editing by leucyl-tRNA synthetase., Lincecum TL Jr, Tukalo M, Yaremchuk A, Mursinna RS, Williams AM, Sproat BS, Van Den Eynde W, Link A, Van Calenbergh S, Grotli M, Martinis SA, Cusack S, Mol Cell. 2003 Apr;11(4):951-63. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12718881 12718881]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
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[[Category: synthetase]]
[[Category: synthetase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:15:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:08:25 2008''

Revision as of 11:08, 20 March 2008


PDB ID 1obc

Drag the structure with the mouse to rotate
, resolution 2.10Å
Sites:
Ligands: , and
Coordinates: save as pdb, mmCIF, xml



LEUCYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH A POST-TRANSFER EDITING SUBSTRATE ANALOGUE


Overview

The aminoacyl-tRNA synthetases link tRNAs with their cognate amino acid. In some cases, their fidelity relies on hydrolytic editing that destroys incorrectly activated amino acids or mischarged tRNAs. We present structures of leucyl-tRNA synthetase complexed with analogs of the distinct pre- and posttransfer editing substrates. The editing active site binds the two different substrates using a single amino acid discriminatory pocket while preserving the same mode of adenine recognition. This suggests a similar mechanism of hydrolysis for both editing substrates that depends on a key, completely conserved aspartic acid, which interacts with the alpha-amino group of the noncognate amino acid and positions both substrates for hydrolysis. Our results demonstrate the economy by which a single active site accommodates two distinct substrates in a proofreading process critical to the fidelity of protein synthesis.

About this Structure

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

Reference

Structural and mechanistic basis of pre- and posttransfer editing by leucyl-tRNA synthetase., Lincecum TL Jr, Tukalo M, Yaremchuk A, Mursinna RS, Williams AM, Sproat BS, Van Den Eynde W, Link A, Van Calenbergh S, Grotli M, Martinis SA, Cusack S, Mol Cell. 2003 Apr;11(4):951-63. PMID:12718881[[Category: atp + l-leucine + trna (leu) -> amp + ppi l-leucyl-trna(leu)]]

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