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1bs2
From Proteopedia
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| - | [[Image:1bs2.gif|left|200px]] | + | [[Image:1bs2.gif|left|200px]] |
| - | + | ||
| - | '''YEAST ARGINYL-TRNA SYNTHETASE''' | + | {{Structure |
| + | |PDB= 1bs2 |SIZE=350|CAPTION= <scene name='initialview01'>1bs2</scene>, resolution 2.75Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ARG:ARGININE'>ARG</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Arginine--tRNA_ligase Arginine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.19 6.1.1.19] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''YEAST ARGINYL-TRNA SYNTHETASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BS2 is a [ | + | 1BS2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BS2 OCA]. |
==Reference== | ==Reference== | ||
| - | L-arginine recognition by yeast arginyl-tRNA synthetase., Cavarelli J, Delagoutte B, Eriani G, Gangloff J, Moras D, EMBO J. 1998 Sep 15;17(18):5438-48. PMID:[http:// | + | L-arginine recognition by yeast arginyl-tRNA synthetase., Cavarelli J, Delagoutte B, Eriani G, Gangloff J, Moras D, EMBO J. 1998 Sep 15;17(18):5438-48. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9736621 9736621] |
[[Category: Arginine--tRNA ligase]] | [[Category: Arginine--tRNA ligase]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
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[[Category: protein biosynthesis]] | [[Category: protein biosynthesis]] | ||
| - | ''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 10:15:02 2008'' |
Revision as of 08:15, 20 March 2008
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| , resolution 2.75Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Arginine--tRNA ligase, with EC number 6.1.1.19 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
YEAST ARGINYL-TRNA SYNTHETASE
Overview
The crystal structure of arginyl-tRNA synthetase (ArgRS) from Saccharomyces cerevisiae, a class I aminoacyl-tRNA synthetase (aaRS), with L-arginine bound to the active site has been solved at 2.75 A resolution and refined to a crystallographic R-factor of 19.7%. ArgRS is composed predominantly of alpha-helices and can be divided into five domains, including the class I-specific active site. The N-terminal domain shows striking similarity to some completely unrelated proteins and defines a module which should participate in specific tRNA recognition. The C-terminal domain, which is the putative anticodon-binding module, displays an all-alpha-helix fold highly similar to that of Escherichia coli methionyl-tRNA synthetase. While ArgRS requires tRNAArg for the first step of the aminoacylation reaction, the results show that its presence is not a prerequisite for L-arginine binding. All H-bond-forming capability of L-arginine is used by the protein for the specific recognition. The guanidinium group forms two salt bridge interactions with two acidic residues, and one H-bond with a tyrosine residue; these three residues are strictly conserved in all ArgRS sequences. This tyrosine is also conserved in other class I aaRS active sites but plays several functional roles. The ArgRS structure allows the definition of a new framework for sequence alignments and subclass definition in class I aaRSs.
About this Structure
1BS2 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
L-arginine recognition by yeast arginyl-tRNA synthetase., Cavarelli J, Delagoutte B, Eriani G, Gangloff J, Moras D, EMBO J. 1998 Sep 15;17(18):5438-48. PMID:9736621
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