4ojm: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
{{STRUCTURE_4ojm| PDB=4ojm | SCENE= }} | |||
===Crystal structure of a C-terminally truncated CYT-18 protein including N-terminal residues=== | |||
{{ABSTRACT_PUBMED_24520960}} | |||
==Function== | |||
[[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. | |||
==About this Structure== | |||
[[4ojm]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OJM OCA]. | |||
==Reference== | |||
<ref group="xtra">PMID:024520960</ref><references group="xtra"/><references/> | |||
[[Category: Tyrosine--tRNA ligase]] | |||
[[Category: Geng, C.]] | |||
[[Category: Paukstelis, P J.]] | |||
[[Category: Ligase]] | |||
[[Category: Splicing]] | |||
[[Category: Trna ligase]] | |||
[[Category: Tyrr]] | |||
Revision as of 09:49, 16 April 2014
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:https://dx.doi.org/10.1021/bi401614h
