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3a5y
From Proteopedia
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{{STRUCTURE_3a5y| PDB=3a5y | SCENE= }} | {{STRUCTURE_3a5y| PDB=3a5y | SCENE= }} | ||
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===Crystal structure of GenX from Escherichia coli in complex with lysyladenylate analog=== | ===Crystal structure of GenX from Escherichia coli in complex with lysyladenylate analog=== | ||
| + | {{ABSTRACT_PUBMED_20729861}} | ||
| - | + | ==Function== | |
| + | [[http://www.uniprot.org/uniprot/C3SGA2_ECOLX C3SGA2_ECOLX]] With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34' (By similarity).[HAMAP-Rule:MF_00174] | ||
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID:020729861</ref><references group="xtra"/> | + | <ref group="xtra">PMID:020729861</ref><references group="xtra"/><references/> |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Lysine--tRNA ligase]] | [[Category: Lysine--tRNA ligase]] | ||
Revision as of 05:26, 23 October 2013
Contents |
Crystal structure of GenX from Escherichia coli in complex with lysyladenylate analog
Template:ABSTRACT PUBMED 20729861
Function
[C3SGA2_ECOLX] With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34' (By similarity).[HAMAP-Rule:MF_00174]
About this Structure
3a5y is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
- Yanagisawa T, Sumida T, Ishii R, Takemoto C, Yokoyama S. A paralog of lysyl-tRNA synthetase aminoacylates a conserved lysine residue in translation elongation factor P. Nat Struct Mol Biol. 2010 Sep;17(9):1136-43. Epub 2010 Aug 22. PMID:20729861 doi:10.1038/nsmb.1889
Categories: Escherichia coli | Lysine--tRNA ligase | Ishii, R. | Sumida, T. | Yanagisawa, T. | Yokoyama, S. | Aminoacyl-trna synthetase | Aminoacyl-trna synthetase paralog | Ligase | Lysyl-trna synthetase | Lysyladenylate analog | National project on protein structural and functional analyse | Nppsfa | Riken structural genomics/proteomics initiative | Rsgi | Structural genomic | Translation | Trna
