2lzj
From Proteopedia
(Difference between revisions)
Line 1: | Line 1: | ||
{{STRUCTURE_2lzj| PDB=2lzj | SCENE= }} | {{STRUCTURE_2lzj| PDB=2lzj | SCENE= }} | ||
===Refined solution structure and dynamics of First Catalytic Cysteine Half-domain from mouse E1 enzyme=== | ===Refined solution structure and dynamics of First Catalytic Cysteine Half-domain from mouse E1 enzyme=== | ||
+ | {{ABSTRACT_PUBMED_24211821}} | ||
==Function== | ==Function== | ||
Line 6: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
- | [[2lzj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | [[2lzj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LZJ OCA]. |
- | [[Category: | + | |
+ | ==Reference== | ||
+ | <ref group="xtra">PMID:024211821</ref><references group="xtra"/><references/> | ||
+ | [[Category: Lk3 transgenic mice]] | ||
[[Category: Bochtler, M.]] | [[Category: Bochtler, M.]] | ||
[[Category: Ejchart, A.]] | [[Category: Ejchart, A.]] |
Revision as of 06:11, 4 December 2013
Contents |
Refined solution structure and dynamics of First Catalytic Cysteine Half-domain from mouse E1 enzyme
Template:ABSTRACT PUBMED 24211821
Function
[UBA1_MOUSE] Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding an ubiquitin-E1 thioester and free AMP.
About this Structure
2lzj is a 1 chain structure with sequence from Lk3 transgenic mice. Full experimental information is available from OCA.
Reference
- Jaremko M, Jaremko L, Nowakowski M, Wojciechowski M, Szczepanowski RH, Panecka R, Zhukov I, Bochtler M, Ejchart A. NMR structural studies of the first catalytic half-domain of ubiquitin activating enzyme. J Struct Biol. 2013 Nov 6. pii: S1047-8477(13)00299-2. doi:, 10.1016/j.jsb.2013.10.020. PMID:24211821 doi:http://dx.doi.org/10.1016/j.jsb.2013.10.020
Categories: Lk3 transgenic mice | Bochtler, M. | Ejchart, A. | Filipek, R. | Jaremko, L. | Jaremko, M. | Nowakowski, M. | Szczepanowski, R H. | Wojciechowski, M. | Beta-barrel architecture | Catalytic half-domain | Flexible thermini | Ligase | Mouse e1 enzyme | Protein degradation | Ubiquitinylation