2o97

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(New page: 200px<br /><applet load="2o97" size="450" color="white" frame="true" align="right" spinBox="true" caption="2o97, resolution 2.45&Aring;" /> '''Crystal Structure of...)
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[[Image:2o97.jpg|left|200px]]<br /><applet load="2o97" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2o97, resolution 2.45&Aring;" />
caption="2o97, resolution 2.45&Aring;" />
'''Crystal Structure of E. coli HU heterodimer'''<br />
'''Crystal Structure of E. coli HU heterodimer'''<br />
==Overview==
==Overview==
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We determined the crystal structure of the Escherichia coli, nucleoid-associated HUalphabeta protein by x-ray diffraction and observed, that the heterodimers form multimers with octameric units in three, potential arrangements, which may serve specialized roles in different DNA, transaction reactions. It is of special importance that one of the, structures forms spiral filaments with left-handed rotations. A negatively, superhelical DNA can be modeled to wrap around this left-handed, HUalphabeta multimer. Whereas the wild-type HU generated negative DNA, supercoiling in vitro, an engineered heterodimer with an altered amino, acid residue critical for the formation of the left-handed spiral protein, in the crystal was defective in the process, thus providing the structural, explanation for the classical property of HU to restrain negative, supercoils in DNA.
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We determined the crystal structure of the Escherichia coli nucleoid-associated HUalphabeta protein by x-ray diffraction and observed that the heterodimers form multimers with octameric units in three potential arrangements, which may serve specialized roles in different DNA transaction reactions. It is of special importance that one of the structures forms spiral filaments with left-handed rotations. A negatively superhelical DNA can be modeled to wrap around this left-handed HUalphabeta multimer. Whereas the wild-type HU generated negative DNA supercoiling in vitro, an engineered heterodimer with an altered amino acid residue critical for the formation of the left-handed spiral protein in the crystal was defective in the process, thus providing the structural explanation for the classical property of HU to restrain negative supercoils in DNA.
==About this Structure==
==About this Structure==
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2O97 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with NI and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2O97 OCA].
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2O97 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=NI:'>NI</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O97 OCA].
==Reference==
==Reference==
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Spiral structure of Escherichia coli HU{alpha}beta provides foundation for DNA supercoiling., Guo F, Adhya S, Proc Natl Acad Sci U S A. 2007 Mar 13;104(11):4309-14. Epub 2007 Mar 5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17360520 17360520]
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Spiral structure of Escherichia coli HUalphabeta provides foundation for DNA supercoiling., Guo F, Adhya S, Proc Natl Acad Sci U S A. 2007 Mar 13;104(11):4309-14. Epub 2007 Mar 5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17360520 17360520]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: heterodimer]]
[[Category: heterodimer]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 13:05:35 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:15:52 2008''

Revision as of 16:15, 21 February 2008

Image:2o97.jpg

2o97, resolution 2.45Å

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Crystal Structure of E. coli HU heterodimer

Overview

We determined the crystal structure of the Escherichia coli nucleoid-associated HUalphabeta protein by x-ray diffraction and observed that the heterodimers form multimers with octameric units in three potential arrangements, which may serve specialized roles in different DNA transaction reactions. It is of special importance that one of the structures forms spiral filaments with left-handed rotations. A negatively superhelical DNA can be modeled to wrap around this left-handed HUalphabeta multimer. Whereas the wild-type HU generated negative DNA supercoiling in vitro, an engineered heterodimer with an altered amino acid residue critical for the formation of the left-handed spiral protein in the crystal was defective in the process, thus providing the structural explanation for the classical property of HU to restrain negative supercoils in DNA.

About this Structure

2O97 is a Protein complex structure of sequences from Escherichia coli with and as ligands. Full crystallographic information is available from OCA.

Reference

Spiral structure of Escherichia coli HUalphabeta provides foundation for DNA supercoiling., Guo F, Adhya S, Proc Natl Acad Sci U S A. 2007 Mar 13;104(11):4309-14. Epub 2007 Mar 5. PMID:17360520

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