1hru: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
New page: left|200px<br /><applet load="1hru" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hru, resolution 2.00Å" /> '''THE STRUCTURE OF THE...
 
No edit summary
Line 1: Line 1:
[[Image:1hru.gif|left|200px]]<br /><applet load="1hru" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1hru.gif|left|200px]]<br /><applet load="1hru" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1hru, resolution 2.00&Aring;" />
caption="1hru, resolution 2.00&Aring;" />
'''THE STRUCTURE OF THE YRDC GENE PRODUCT FROM E.COLI'''<br />
'''THE STRUCTURE OF THE YRDC GENE PRODUCT FROM E.COLI'''<br />


==Overview==
==Overview==
The yrdC family of genes codes for proteins that occur both independently, and as a domain in proteins that have been implicated in regulation. An, example for the latter case is the sua5 gene from yeast. SuaS was, identified as a suppressor of a translation initiation defect in, cytochrome c and is required for normal growth in yeast (Na JG, Pinto I, Hampsey M, 1992, Genetics 11:791-801). However, the function of the Sua5, protein remains unknown; Sua5 could act either at the transcriptional or, the posttranscriptional levels to compensate for an aberrant translation, start codon in the cyc gene. To potentially learn more about the function, of YrdC and proteins featuring this domain, the crystal structure of the, YrdC protein from Escherichia coli was determined at a resolution of 2.0, A. YrdC adopts a new fold with no obvious similarity to those of other, proteins with known three-dimensional (3D) structure. The protein features, a large concave surface on one side that exhibits a positive electrostatic, potential. The dimensions of this depression, its curvature, and the fact, that conserved basic amino acids are located at its floor suggest that, YrdC may be a nucleic acid binding protein. An investigation of YrdC's, binding affinities for single- and double-stranded RNA and DNA fragments, as well as tRNAs demonstrates that YrdC binds preferentially to, double-stranded RNA. Our work provides evidence that 3D structures of, functionally uncharacterized gene products with unique sequences can yield, novel folds and functional insights.
The yrdC family of genes codes for proteins that occur both independently and as a domain in proteins that have been implicated in regulation. An example for the latter case is the sua5 gene from yeast. SuaS was identified as a suppressor of a translation initiation defect in cytochrome c and is required for normal growth in yeast (Na JG, Pinto I, Hampsey M, 1992, Genetics 11:791-801). However, the function of the Sua5 protein remains unknown; Sua5 could act either at the transcriptional or the posttranscriptional levels to compensate for an aberrant translation start codon in the cyc gene. To potentially learn more about the function of YrdC and proteins featuring this domain, the crystal structure of the YrdC protein from Escherichia coli was determined at a resolution of 2.0 A. YrdC adopts a new fold with no obvious similarity to those of other proteins with known three-dimensional (3D) structure. The protein features a large concave surface on one side that exhibits a positive electrostatic potential. The dimensions of this depression, its curvature, and the fact that conserved basic amino acids are located at its floor suggest that YrdC may be a nucleic acid binding protein. An investigation of YrdC's binding affinities for single- and double-stranded RNA and DNA fragments as well as tRNAs demonstrates that YrdC binds preferentially to double-stranded RNA. Our work provides evidence that 3D structures of functionally uncharacterized gene products with unique sequences can yield novel folds and functional insights.


==About this Structure==
==About this Structure==
1HRU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HRU OCA].  
1HRU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HRU OCA].  


==Reference==
==Reference==
Line 13: Line 13:
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Anderson, W.F.]]
[[Category: Anderson, W F.]]
[[Category: Bushueva, T.]]
[[Category: Bushueva, T.]]
[[Category: Egli, M.]]
[[Category: Egli, M.]]
[[Category: Joachimiak, A.]]
[[Category: Joachimiak, A.]]
[[Category: MCSG, Midwest.Center.for.Structural.Genomics.]]
[[Category: MCSG, Midwest Center for Structural Genomics.]]
[[Category: Sanishvili, R.]]
[[Category: Sanishvili, R.]]
[[Category: Teplova, M.]]
[[Category: Teplova, M.]]
Line 32: Line 32:
[[Category: yrdc]]
[[Category: yrdc]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:47:32 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:04:13 2008''

Revision as of 14:04, 21 February 2008

File:1hru.gif


1hru, resolution 2.00Å

Drag the structure with the mouse to rotate

THE STRUCTURE OF THE YRDC GENE PRODUCT FROM E.COLI

OverviewOverview

The yrdC family of genes codes for proteins that occur both independently and as a domain in proteins that have been implicated in regulation. An example for the latter case is the sua5 gene from yeast. SuaS was identified as a suppressor of a translation initiation defect in cytochrome c and is required for normal growth in yeast (Na JG, Pinto I, Hampsey M, 1992, Genetics 11:791-801). However, the function of the Sua5 protein remains unknown; Sua5 could act either at the transcriptional or the posttranscriptional levels to compensate for an aberrant translation start codon in the cyc gene. To potentially learn more about the function of YrdC and proteins featuring this domain, the crystal structure of the YrdC protein from Escherichia coli was determined at a resolution of 2.0 A. YrdC adopts a new fold with no obvious similarity to those of other proteins with known three-dimensional (3D) structure. The protein features a large concave surface on one side that exhibits a positive electrostatic potential. The dimensions of this depression, its curvature, and the fact that conserved basic amino acids are located at its floor suggest that YrdC may be a nucleic acid binding protein. An investigation of YrdC's binding affinities for single- and double-stranded RNA and DNA fragments as well as tRNAs demonstrates that YrdC binds preferentially to double-stranded RNA. Our work provides evidence that 3D structures of functionally uncharacterized gene products with unique sequences can yield novel folds and functional insights.

About this StructureAbout this Structure

1HRU is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

The structure of the yrdC gene product from Escherichia coli reveals a new fold and suggests a role in RNA binding., Teplova M, Tereshko V, Sanishvili R, Joachimiak A, Bushueva T, Anderson WF, Egli M, Protein Sci. 2000 Dec;9(12):2557-66. PMID:11206077

Page seeded by OCA on Thu Feb 21 13:04:13 2008

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

OCA