1vce
From Proteopedia
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{{STRUCTURE_1vce| PDB=1vce | SCENE= }} | {{STRUCTURE_1vce| PDB=1vce | SCENE= }} | ||
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===Crystal structure of project ID PH0725 from Pyrococcus horikoshii OT3=== | ===Crystal structure of project ID PH0725 from Pyrococcus horikoshii OT3=== | ||
+ | ==Function== | ||
+ | [[http://www.uniprot.org/uniprot/DPHB_PYRHO DPHB_PYRHO]] S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.<ref>PMID:20873788</ref> | ||
==About this Structure== | ==About this Structure== | ||
[[1vce]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VCE OCA]. | [[1vce]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VCE OCA]. | ||
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+ | ==See Also== | ||
+ | *[[Diphthine synthase|Diphthine synthase]] | ||
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+ | ==Reference== | ||
+ | <references group="xtra"/><references/> | ||
[[Category: Diphthine synthase]] | [[Category: Diphthine synthase]] | ||
[[Category: Pyrococcus horikoshii]] | [[Category: Pyrococcus horikoshii]] |
Revision as of 08:12, 23 April 2014
Contents |
Crystal structure of project ID PH0725 from Pyrococcus horikoshii OT3
Function
[DPHB_PYRHO] S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis.[1]
About this Structure
1vce is a 2 chain structure with sequence from Pyrococcus horikoshii. Full crystallographic information is available from OCA.
See Also
Reference
- ↑ Zhu X, Kim J, Su X, Lin H. Reconstitution of diphthine synthase activity in vitro. Biochemistry. 2010 Nov 9;49(44):9649-57. doi: 10.1021/bi100812h. PMID:20873788 doi:http://dx.doi.org/10.1021/bi100812h