1asz
From Proteopedia
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| - | [[Image:1asz.gif|left|200px]] | + | [[Image:1asz.gif|left|200px]] |
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| - | '''THE ACTIVE SITE OF YEAST ASPARTYL-TRNA SYNTHETASE: STRUCTURAL AND FUNCTIONAL ASPECTS OF THE AMINOACYLATION REACTION''' | + | {{Structure |
| + | |PDB= 1asz |SIZE=350|CAPTION= <scene name='initialview01'>1asz</scene>, resolution 3.0Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Aspartate--tRNA_ligase Aspartate--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.12 6.1.1.12] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''THE ACTIVE SITE OF YEAST ASPARTYL-TRNA SYNTHETASE: STRUCTURAL AND FUNCTIONAL ASPECTS OF THE AMINOACYLATION REACTION''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ASZ is a [ | + | 1ASZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. The following page contains interesting information on the relation of 1ASZ with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb16_1.html Aminoacyl-tRNA Synthetases]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ASZ OCA]. |
==Reference== | ==Reference== | ||
| - | The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation reaction., Cavarelli J, Eriani G, Rees B, Ruff M, Boeglin M, Mitschler A, Martin F, Gangloff J, Thierry JC, Moras D, EMBO J. 1994 Jan 15;13(2):327-37. PMID:[http:// | + | The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation reaction., Cavarelli J, Eriani G, Rees B, Ruff M, Boeglin M, Mitschler A, Martin F, Gangloff J, Thierry JC, Moras D, EMBO J. 1994 Jan 15;13(2):327-37. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8313877 8313877] |
[[Category: Aminoacyl-tRNA Synthetases]] | [[Category: Aminoacyl-tRNA Synthetases]] | ||
[[Category: Aspartate--tRNA ligase]] | [[Category: Aspartate--tRNA ligase]] | ||
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[[Category: complex (aminoacyl-trna synthase/trna)]] | [[Category: complex (aminoacyl-trna synthase/trna)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:01:53 2008'' |
Revision as of 08:01, 20 March 2008
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| , resolution 3.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Aspartate--tRNA ligase, with EC number 6.1.1.12 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE ACTIVE SITE OF YEAST ASPARTYL-TRNA SYNTHETASE: STRUCTURAL AND FUNCTIONAL ASPECTS OF THE AMINOACYLATION REACTION
Overview
The crystal structures of the various complexes formed by yeast aspartyl-tRNA synthetase (AspRS) and its substrates provide snapshots of the active site corresponding to different steps of the aminoacylation reaction. Native crystals of the binary complex tRNA-AspRS were soaked in solutions containing the two other substrates, ATP (or its analog AMPPcP) and aspartic acid. When all substrates are present in the crystal, this leads to the formation of the aspartyl-adenylate and/or the aspartyl-tRNA. A class II-specific pathway for the aminoacylation reaction is proposed which explains the known functional differences between the two classes while preserving a common framework. Extended signature sequences characteristic of class II aaRS (motifs 2 and 3) constitute the basic functional unit. The ATP molecule adopts a bent conformation, stabilized by the invariant Arg531 of motif 3 and a magnesium ion coordinated to the pyrophosphate group and to two class-invariant acidic residues. The aspartic acid substrate is positioned by a class II invariant acidic residue, Asp342, interacting with the amino group and by amino acids conserved in the aspartyl synthetase family. The amino acids in contact with the substrates have been probed by site-directed mutagenesis for their functional implication.
About this Structure
1ASZ is a Single protein structure of sequence from Saccharomyces cerevisiae. The following page contains interesting information on the relation of 1ASZ with [Aminoacyl-tRNA Synthetases]. Full crystallographic information is available from OCA.
Reference
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation reaction., Cavarelli J, Eriani G, Rees B, Ruff M, Boeglin M, Mitschler A, Martin F, Gangloff J, Thierry JC, Moras D, EMBO J. 1994 Jan 15;13(2):327-37. PMID:8313877
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