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New page: left|200px<br /><applet load="1kaw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kaw, resolution 2.9Å" /> '''STRUCTURE OF SINGLE S...
 
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[[Image:1kaw.jpg|left|200px]]<br /><applet load="1kaw" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1kaw.jpg|left|200px]]<br /><applet load="1kaw" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1kaw, resolution 2.9&Aring;" />
caption="1kaw, resolution 2.9&Aring;" />
'''STRUCTURE OF SINGLE STRANDED DNA BINDING PROTEIN (SSB)'''<br />
'''STRUCTURE OF SINGLE STRANDED DNA BINDING PROTEIN (SSB)'''<br />


==Overview==
==Overview==
The crystal structure of the tetrameric DNA-binding domain of the, single-stranded DNA binding protein from Escherichia coli was determined, at a resolution of 2.9 A using multiwavelength anomalous dispersion. Each, monomer in the tetramer is topologically similar to an oligomer-binding, fold. Two monomers each contribute three beta-strands to a single, six-stranded beta-sheet to form a dimer. Two dimer-dimer interfaces are, observed within the crystal. One of these stabilizes the tetramer in, solution. The other interface promotes a superhelical structure within the, crystal that may reflect tetramer-tetramer interactions involved in the, positive cooperative binding of the single-stranded DNA-binding protein to, single-stranded DNA.
The crystal structure of the tetrameric DNA-binding domain of the single-stranded DNA binding protein from Escherichia coli was determined at a resolution of 2.9 A using multiwavelength anomalous dispersion. Each monomer in the tetramer is topologically similar to an oligomer-binding fold. Two monomers each contribute three beta-strands to a single six-stranded beta-sheet to form a dimer. Two dimer-dimer interfaces are observed within the crystal. One of these stabilizes the tetramer in solution. The other interface promotes a superhelical structure within the crystal that may reflect tetramer-tetramer interactions involved in the positive cooperative binding of the single-stranded DNA-binding protein to single-stranded DNA.


==About this Structure==
==About this Structure==
1KAW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KAW OCA].  
1KAW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KAW OCA].  


==Reference==
==Reference==
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[[Category: ssb]]
[[Category: ssb]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:00:37 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:32:00 2008''

Revision as of 11:32, 21 February 2008

File:1kaw.jpg


1kaw, resolution 2.9Å

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STRUCTURE OF SINGLE STRANDED DNA BINDING PROTEIN (SSB)

Overview

The crystal structure of the tetrameric DNA-binding domain of the single-stranded DNA binding protein from Escherichia coli was determined at a resolution of 2.9 A using multiwavelength anomalous dispersion. Each monomer in the tetramer is topologically similar to an oligomer-binding fold. Two monomers each contribute three beta-strands to a single six-stranded beta-sheet to form a dimer. Two dimer-dimer interfaces are observed within the crystal. One of these stabilizes the tetramer in solution. The other interface promotes a superhelical structure within the crystal that may reflect tetramer-tetramer interactions involved in the positive cooperative binding of the single-stranded DNA-binding protein to single-stranded DNA.

About this Structure

1KAW is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structure of the homo-tetrameric DNA binding domain of Escherichia coli single-stranded DNA-binding protein determined by multiwavelength x-ray diffraction on the selenomethionyl protein at 2.9-A resolution., Raghunathan S, Ricard CS, Lohman TM, Waksman G, Proc Natl Acad Sci U S A. 1997 Jun 24;94(13):6652-7. PMID:9192620

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