1lr1: Difference between revisions
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'''Solution Structure of the Oligomerization Domain of the Bacterial Chromatin-Structuring Protein H-NS'''<br /> | '''Solution Structure of the Oligomerization Domain of the Bacterial Chromatin-Structuring Protein H-NS'''<br /> | ||
==Overview== | ==Overview== | ||
H-NS plays a role in condensing DNA in the bacterial nucleoid. This 136 | H-NS plays a role in condensing DNA in the bacterial nucleoid. This 136 amino acid protein comprises two functional domains separated by a flexible linker. High order structures formed by the N-terminal oligomerization domain (residues 1-89) constitute the basis of a protein scaffold that binds DNA via the C-terminal domain. Deletion of residues 57-89 or 64-89 of the oligomerization domain precludes high order structure formation, yielding a discrete dimer. This dimerization event represents the initial event in the formation of high order structure. The dimers thus constitute the basic building block of the protein scaffold. The three-dimensional solution structure of one of these units (residues 1-57) has been determined. Activity of these structural units is demonstrated by a dominant negative effect on high order structure formation on addition to the full length protein. Truncated and site-directed mutant forms of the N-terminal domain of H-NS reveal how the dimeric unit self-associates in a head-to-tail manner and demonstrate the importance of secondary structure in this interaction to form high order structures. A model is presented for the structural basis for DNA packaging in bacterial cells. | ||
==About this Structure== | ==About this Structure== | ||
1LR1 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:// | 1LR1 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=1LR1 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Driscoll, P | [[Category: Driscoll, P C.]] | ||
[[Category: Eccleston, J.]] | [[Category: Eccleston, J.]] | ||
[[Category: Esposito, D.]] | [[Category: Esposito, D.]] | ||
[[Category: Haq, I.]] | [[Category: Haq, I.]] | ||
[[Category: Harris, R.]] | [[Category: Harris, R.]] | ||
[[Category: Higgins, C | [[Category: Higgins, C F.]] | ||
[[Category: Hinton, J | [[Category: Hinton, J C.D.]] | ||
[[Category: Ladbury, J | [[Category: Ladbury, J E.]] | ||
[[Category: Mbabaali, A.]] | [[Category: Mbabaali, A.]] | ||
[[Category: Ono, S.]] | [[Category: Ono, S.]] | ||
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[[Category: nucleoid assembly]] | [[Category: nucleoid assembly]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:47:37 2008'' | ||
Revision as of 11:47, 21 February 2008
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Solution Structure of the Oligomerization Domain of the Bacterial Chromatin-Structuring Protein H-NS
Overview
H-NS plays a role in condensing DNA in the bacterial nucleoid. This 136 amino acid protein comprises two functional domains separated by a flexible linker. High order structures formed by the N-terminal oligomerization domain (residues 1-89) constitute the basis of a protein scaffold that binds DNA via the C-terminal domain. Deletion of residues 57-89 or 64-89 of the oligomerization domain precludes high order structure formation, yielding a discrete dimer. This dimerization event represents the initial event in the formation of high order structure. The dimers thus constitute the basic building block of the protein scaffold. The three-dimensional solution structure of one of these units (residues 1-57) has been determined. Activity of these structural units is demonstrated by a dominant negative effect on high order structure formation on addition to the full length protein. Truncated and site-directed mutant forms of the N-terminal domain of H-NS reveal how the dimeric unit self-associates in a head-to-tail manner and demonstrate the importance of secondary structure in this interaction to form high order structures. A model is presented for the structural basis for DNA packaging in bacterial cells.
About this Structure
1LR1 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
H-NS oligomerization domain structure reveals the mechanism for high order self-association of the intact protein., Esposito D, Petrovic A, Harris R, Ono S, Eccleston JF, Mbabaali A, Haq I, Higgins CF, Hinton JC, Driscoll PC, Ladbury JE, J Mol Biol. 2002 Dec 6;324(4):841-50. PMID:12460581
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