This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


3bca

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:3bca.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:3bca.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_3bca| PDB=3bca | SCENE= }}
{{STRUCTURE_3bca| PDB=3bca | SCENE= }}
-
'''Crystal structure of mouse selenocysteine synthase, sodium iodide soak'''
+
===Crystal structure of mouse selenocysteine synthase, sodium iodide soak===
-
==Overview==
+
<!--
-
In eukaryotes and Archaea, selenocysteine synthase (SecS) converts O-phospho-l-seryl-tRNA([Ser]Sec) into selenocysteyl-tRNA([Ser]Sec) using selenophosphate as the selenium donor compound. The molecular mechanisms underlying SecS activity are presently unknown. We have delineated a 450-residue core of mouse SecS, which retained full selenocysteyl-tRNA([Ser]Sec) synthesis activity, and determined its crystal structure at 1.65A resolution. SecS exhibits three domains that place it in the fold type I family of pyridoxal phosphate (PLP)-dependent enzymes. Two SecS monomers interact intimately and together build up two identical active sites around PLP in a Schiff-base linkage with lysine 284. Two SecS dimers further associate to form a homotetramer. The N terminus, which mediates tetramer formation, and a large insertion that remodels the active site set SecS aside from other members of the family. The active site insertion contributes to PLP binding and positions a glutamate next to the PLP, where it could repel substrates with a free alpha-carboxyl group, suggesting why SecS does not act on free O-phospho-l-serine. Upon soaking crystals in phosphate buffer, a previously disordered loop within the active site insertion contracted to form a phosphate binding site. Residues that are strictly conserved in SecS orthologs but variant in related enzymes coordinate the phosphate and upon mutation corrupt SecS activity. Modeling suggested that the phosphate loop accommodates the gamma-phosphate moiety of O-phospho-l-seryl-tRNA([Ser]Sec) and, after phosphate elimination, binds selenophosphate to initiate attack on the proposed aminoacrylyl-tRNA([Ser]Sec) intermediate. Based on these results and on the activity profiles of mechanism-based inhibitors, we offer a detailed reaction mechanism for the enzyme.
+
The line below this paragraph, {{ABSTRACT_PUBMED_18093968}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 18093968 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_18093968}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Transferase]]
[[Category: Transferase]]
[[Category: X-ray crystallography]]
[[Category: X-ray crystallography]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:37:43 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:07:58 2008''

Revision as of 21:08, 27 July 2008

Image:3bca.png

Template:STRUCTURE 3bca

Crystal structure of mouse selenocysteine synthase, sodium iodide soak

Template:ABSTRACT PUBMED 18093968

About this Structure

3BCA is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Structure and catalytic mechanism of eukaryotic selenocysteine synthase., Ganichkin OM, Xu XM, Carlson BA, Mix H, Hatfield DL, Gladyshev VN, Wahl MC, J Biol Chem. 2008 Feb 29;283(9):5849-65. Epub 2007 Dec 19. PMID:18093968

Page seeded by OCA on Mon Jul 28 00:07:58 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3bca"
Personal tools