1s7o

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(New page: 200px<br /><applet load="1s7o" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s7o, resolution 2.31&Aring;" /> '''Crystal structure of...)
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[[Image:1s7o.gif|left|200px]]<br /><applet load="1s7o" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1s7o.gif|left|200px]]<br /><applet load="1s7o" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1s7o, resolution 2.31&Aring;" />
caption="1s7o, resolution 2.31&Aring;" />
'''Crystal structure of putative DNA binding protein SP_1288 from Streptococcus pygenes'''<br />
'''Crystal structure of putative DNA binding protein SP_1288 from Streptococcus pygenes'''<br />
==Overview==
==Overview==
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The crystal structure of the putative DNA-binding protein SP_1288, (gi/15675166, also listed as gi/28895954) from Streptococcus pyogenes has, been determined by X-ray crystallography to a resolution of 2.3 A using, anomalous diffraction data at the Se peak wavelength. SP_1288 belongs to a, family of proteins whose cellular function is associated with the signal, recognition particle; no structural information has been available until, now about the members of the family. Crystallographic analysis revealed, that the overall fold of SP_1288 consists exclusively of alpha-helices and, that 75% of the structure has good similarity to domain 4 of the sigma, subunit of RNA polymerase. This suggests its possible involvement in the, biochemical function of transcription initiation, which includes, interaction with DNA.
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The crystal structure of the putative DNA-binding protein SP_1288 (gi/15675166, also listed as gi/28895954) from Streptococcus pyogenes has been determined by X-ray crystallography to a resolution of 2.3 A using anomalous diffraction data at the Se peak wavelength. SP_1288 belongs to a family of proteins whose cellular function is associated with the signal recognition particle; no structural information has been available until now about the members of the family. Crystallographic analysis revealed that the overall fold of SP_1288 consists exclusively of alpha-helices and that 75% of the structure has good similarity to domain 4 of the sigma subunit of RNA polymerase. This suggests its possible involvement in the biochemical function of transcription initiation, which includes interaction with DNA.
==About this Structure==
==About this Structure==
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1S7O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1S7O OCA].
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1S7O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S7O OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Streptococcus pyogenes]]
[[Category: Streptococcus pyogenes]]
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[[Category: BSGC, Berkeley.Structural.Genomics.Center.]]
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[[Category: BSGC, Berkeley Structural Genomics Center.]]
[[Category: DeGiovanni, A.]]
[[Category: DeGiovanni, A.]]
[[Category: Kim, R.]]
[[Category: Kim, R.]]
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[[Category: Kim, S.H.]]
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[[Category: Kim, S H.]]
[[Category: Oganesyan, V.]]
[[Category: Oganesyan, V.]]
[[Category: Pufan, R.]]
[[Category: Pufan, R.]]
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[[Category: x-rat crystallography]]
[[Category: x-rat crystallography]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:10:28 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:58:49 2008''

Revision as of 12:58, 21 February 2008


1s7o, resolution 2.31Å

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Crystal structure of putative DNA binding protein SP_1288 from Streptococcus pygenes

Overview

The crystal structure of the putative DNA-binding protein SP_1288 (gi/15675166, also listed as gi/28895954) from Streptococcus pyogenes has been determined by X-ray crystallography to a resolution of 2.3 A using anomalous diffraction data at the Se peak wavelength. SP_1288 belongs to a family of proteins whose cellular function is associated with the signal recognition particle; no structural information has been available until now about the members of the family. Crystallographic analysis revealed that the overall fold of SP_1288 consists exclusively of alpha-helices and that 75% of the structure has good similarity to domain 4 of the sigma subunit of RNA polymerase. This suggests its possible involvement in the biochemical function of transcription initiation, which includes interaction with DNA.

About this Structure

1S7O is a Single protein structure of sequence from Streptococcus pyogenes. Full crystallographic information is available from OCA.

Reference

Structure of the putative DNA-binding protein SP_1288 from Streptococcus pyogenes., Oganesyan V, Pufan R, DeGiovanni A, Yokota H, Kim R, Kim SH, Acta Crystallogr D Biol Crystallogr. 2004 Jul;60(Pt 7):1266-71. Epub 2004, Jun 22. PMID:15213388

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