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| - | [[Image:1bs2.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1bs2.png|left|200px]] |
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| | {{STRUCTURE_1bs2| PDB=1bs2 | SCENE= }} | | {{STRUCTURE_1bs2| PDB=1bs2 | SCENE= }} |
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| - | '''YEAST ARGINYL-TRNA SYNTHETASE'''
| + | ===YEAST ARGINYL-TRNA SYNTHETASE=== |
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| - | ==Overview==
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| - | 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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_9736621}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 9736621 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_9736621}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Ligase]] | | [[Category: Ligase]] |
| | [[Category: Protein biosynthesis]] | | [[Category: Protein biosynthesis]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:53:15 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:38:11 2008'' |
Revision as of 16:38, 30 June 2008
Template:STRUCTURE 1bs2
YEAST ARGINYL-TRNA SYNTHETASE
Template:ABSTRACT PUBMED 9736621
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
Page seeded by OCA on Mon Jun 30 19:38:11 2008
