3w1h: Difference between revisions

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'''Unreleased structure'''
{{STRUCTURE_3w1h|  PDB=3w1h  |  SCENE=  }}
===Crystal structure of the selenocysteine synthase SelA from Aquifex aeolicus===
{{ABSTRACT_PUBMED_23559248}}


The entry 3w1h is ON HOLD  until Paper Publication
==Function==
[[http://www.uniprot.org/uniprot/SELA_AQUAE SELA_AQUAE]] Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis (By similarity).


Authors: Itoh, Y., Sekine, S., Yokoyama, S.
==About this Structure==
[[3w1h]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus_vf5 Aquifex aeolicus vf5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W1H OCA].  


Description: Crystal structure of the selenocysteine synthase SelA from Aquifex aeolicus
==Reference==
<ref group="xtra">PMID:023559248</ref><references group="xtra"/><references/>
[[Category: Aquifex aeolicus vf5]]
[[Category: Itoh, Y.]]
[[Category: Sekine, S.]]
[[Category: Yokoyama, S.]]
[[Category: Homodecamer]]
[[Category: Pentamer of dimer]]
[[Category: Selenium metabolism]]
[[Category: Selenocysteine synthesis]]
[[Category: Transferase]]

Revision as of 18:09, 19 June 2013

Template:STRUCTURE 3w1h

Crystal structure of the selenocysteine synthase SelA from Aquifex aeolicusCrystal structure of the selenocysteine synthase SelA from Aquifex aeolicus

Template:ABSTRACT PUBMED 23559248

FunctionFunction

[SELA_AQUAE] Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis (By similarity).

About this StructureAbout this Structure

3w1h is a 5 chain structure with sequence from Aquifex aeolicus vf5. Full crystallographic information is available from OCA.

ReferenceReference

[xtra 1]

  1. Itoh Y, Brocker MJ, Sekine S, Hammond G, Suetsugu S, Soll D, Yokoyama S. Decameric SelA*tRNA(Sec) ring structure reveals mechanism of bacterial selenocysteine formation. Science. 2013 Apr 5;340(6128):75-8. doi: 10.1126/science.1229521. PMID:23559248 doi:10.1126/science.1229521

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