2hsn: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 1: Line 1:
[[Image:2hsn.jpg|left|200px]]<br /><applet load="2hsn" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2hsn.jpg|left|200px]]
caption="2hsn, resolution 2.20&Aring;" />
 
'''Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub-complexes'''<br />
{{Structure
|PDB= 2hsn |SIZE=350|CAPTION= <scene name='initialview01'>2hsn</scene>, resolution 2.20&Aring;
|SITE=
|LIGAND=
|ACTIVITY= [http://en.wikipedia.org/wiki/Methionine--tRNA_ligase Methionine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.10 6.1.1.10]
|GENE= MES1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]), ARC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
}}
 
'''Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub-complexes'''
 


==Overview==
==Overview==
Line 7: Line 16:


==About this Structure==
==About this Structure==
2HSN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Active as [http://en.wikipedia.org/wiki/Methionine--tRNA_ligase Methionine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.10 6.1.1.10] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HSN OCA].  
2HSN is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HSN OCA].  


==Reference==
==Reference==
Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub-complexes., Simader H, Hothorn M, Kohler C, Basquin J, Simos G, Suck D, Nucleic Acids Res. 2006;34(14):3968-79. Epub 2006 Aug 12. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16914447 16914447]
Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub-complexes., Simader H, Hothorn M, Kohler C, Basquin J, Simos G, Suck D, Nucleic Acids Res. 2006;34(14):3968-79. Epub 2006 Aug 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16914447 16914447]
[[Category: Methionine--tRNA ligase]]
[[Category: Methionine--tRNA ligase]]
[[Category: Protein complex]]
[[Category: Protein complex]]
Line 20: Line 29:
[[Category: protein complex protein interaction gst-fold]]
[[Category: protein complex protein interaction gst-fold]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:45:20 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:21:07 2008''

Revision as of 18:21, 20 March 2008

File:2hsn.jpg


PDB ID 2hsn

Drag the structure with the mouse to rotate
, resolution 2.20Å
Gene: MES1 (Saccharomyces cerevisiae), ARC1 (Saccharomyces cerevisiae)
Activity: Methionine--tRNA ligase, with EC number 6.1.1.10
Coordinates: save as pdb, mmCIF, xml



Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub-complexes


OverviewOverview

The yeast aminoacyl-tRNA synthetase (aaRS) complex is formed by the methionyl- and glutamyl-tRNA synthetases (MetRS and GluRS, respectively) and the tRNA aminoacylation cofactor Arc1p. It is considered an evolutionary intermediate between prokaryotic aaRS and the multi- aaRS complex found in higher eukaryotes. While a wealth of structural information is available on the enzymatic domains of single aaRS, insight into complex formation between eukaryotic aaRS and associated protein cofactors is missing. Here we report crystal structures of the binary complexes between the interacting domains of Arc1p and MetRS as well as those of Arc1p and GluRS at resolutions of 2.2 and 2.05 A, respectively. The data provide a complete structural model for ternary complex formation between the interacting domains of MetRS, GluRS and Arc1p. The structures reveal that all three domains adopt a glutathione S-transferase (GST)-like fold and that simultaneous interaction of Arc1p with GluRS and MetRS is mediated by the use of a novel interface in addition to a classical GST dimerization interaction. The results demonstrate a novel role for this fold as a heteromerization domain specific to eukaryotic aaRS, associated proteins and protein translation elongation factors.

About this StructureAbout this Structure

2HSN is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub-complexes., Simader H, Hothorn M, Kohler C, Basquin J, Simos G, Suck D, Nucleic Acids Res. 2006;34(14):3968-79. Epub 2006 Aug 12. PMID:16914447

Page seeded by OCA on Thu Mar 20 17:21:07 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA