1t1v
From Proteopedia
(New page: 200px<br /><applet load="1t1v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t1v, resolution 1.60Å" /> '''Crystal Structure of...) |
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| - | [[Image:1t1v.jpg|left|200px]]<br /><applet load="1t1v" size=" | + | [[Image:1t1v.jpg|left|200px]]<br /><applet load="1t1v" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1t1v, resolution 1.60Å" /> | caption="1t1v, resolution 1.60Å" /> | ||
'''Crystal Structure of the Glutaredoxin-like Protein SH3BGRL3 at 1.6 A resolution'''<br /> | '''Crystal Structure of the Glutaredoxin-like Protein SH3BGRL3 at 1.6 A resolution'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We report the 1.6 Angstrom resolution crystal structure of SH3BGRL3, a | + | We report the 1.6 Angstrom resolution crystal structure of SH3BGRL3, a member of a new mammalian protein family of unknown function. The observed "thioredoxin fold" of SH3BGRL3 matches the tertiary structure of glutaredoxins, even in the N-terminal region where the sequence similarity between the two protein families is negligible. In particular, SH3BGRL3 displays structural modifications at the N-terminal Cys-x-x-Cys loop, responsible for glutathione binding and catalysis in glutaredoxins. The loop hosts a six residue insertion, yielding an extra N-terminal-capped helical turn, first observed here for the thioredoxin fold. This, together with deletion of both Cys residues, results in a substantial reshaping of the neighboring cleft, where glutathione is hosted in glutaredoxins. While not active in redox reaction and glutathione binding, SH3BGRL3 may act as an endogenous modulator of glutaredoxin activities by competing, with its fully conserved thioredoxin fold, for binding to yet unknown target proteins. |
==About this Structure== | ==About this Structure== | ||
| - | 1T1V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with SO4, ACY and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1T1V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=ACY:'>ACY</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T1V OCA]. |
==Reference== | ==Reference== | ||
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[[Category: glutaredoxin; thioredoxin fold; protein 3d-structure; x-ray crystallography]] | [[Category: glutaredoxin; thioredoxin fold; protein 3d-structure; x-ray crystallography]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:08:57 2008'' |
Revision as of 13:09, 21 February 2008
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Crystal Structure of the Glutaredoxin-like Protein SH3BGRL3 at 1.6 A resolution
Overview
We report the 1.6 Angstrom resolution crystal structure of SH3BGRL3, a member of a new mammalian protein family of unknown function. The observed "thioredoxin fold" of SH3BGRL3 matches the tertiary structure of glutaredoxins, even in the N-terminal region where the sequence similarity between the two protein families is negligible. In particular, SH3BGRL3 displays structural modifications at the N-terminal Cys-x-x-Cys loop, responsible for glutathione binding and catalysis in glutaredoxins. The loop hosts a six residue insertion, yielding an extra N-terminal-capped helical turn, first observed here for the thioredoxin fold. This, together with deletion of both Cys residues, results in a substantial reshaping of the neighboring cleft, where glutathione is hosted in glutaredoxins. While not active in redox reaction and glutathione binding, SH3BGRL3 may act as an endogenous modulator of glutaredoxin activities by competing, with its fully conserved thioredoxin fold, for binding to yet unknown target proteins.
About this Structure
1T1V is a Single protein structure of sequence from Mus musculus with , and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of the glutaredoxin-like protein SH3BGRL3 at 1.6 Angstrom resolution., Nardini M, Mazzocco M, Massaro A, Maffei M, Vergano A, Donadini A, Scartezzini P, Bolognesi M, Biochem Biophys Res Commun. 2004 May 28;318(2):470-6. PMID:15120624
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