4ojm

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'''Unreleased structure'''
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{{STRUCTURE_4ojm| PDB=4ojm | SCENE= }}
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===Crystal structure of a C-terminally truncated CYT-18 protein including N-terminal residues===
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{{ABSTRACT_PUBMED_24520960}}
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The entry 4ojm is ON HOLD
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==Function==
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[[http://www.uniprot.org/uniprot/SYYM_NEUCR SYYM_NEUCR]] Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). Has both an aminoacyl-tRNA synthetase activity and is involved in the splicing of group I introns. It acts in intron splicing by stabilizing the catalytically active structure of the intron.
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Authors: Paukstelis, P.J., Geng, C.
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==About this Structure==
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[[4ojm]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OJM OCA].
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Description: Crystal structure of a C-terminally truncated CYT-18 protein including N-terminal residues
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==Reference==
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<ref group="xtra">PMID:024520960</ref><references group="xtra"/><references/>
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[[Category: Tyrosine--tRNA ligase]]
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[[Category: Geng, C.]]
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[[Category: Paukstelis, P J.]]
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[[Category: Ligase]]
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[[Category: Splicing]]
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[[Category: Trna ligase]]
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[[Category: Tyrr]]

Revision as of 09:49, 16 April 2014

Template:STRUCTURE 4ojm

Contents

Crystal structure of a C-terminally truncated CYT-18 protein including N-terminal residues

Template:ABSTRACT PUBMED 24520960

Function

[SYYM_NEUCR] Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). Has both an aminoacyl-tRNA synthetase activity and is involved in the splicing of group I introns. It acts in intron splicing by stabilizing the catalytically active structure of the intron.

About this Structure

4ojm is a 1 chain structure. Full crystallographic information is available from OCA.

Reference

  • Geng C, Paukstelis PJ. An in vitro peptide complementation assay for CYT-18-dependent group I intron splicing reveals a new role for the N-terminus. Biochemistry. 2014 Mar 4;53(8):1311-9. doi: 10.1021/bi401614h. Epub 2014 Feb 24. PMID:24520960 doi:http://dx.doi.org/10.1021/bi401614h

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OCA

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