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1lr1
From Proteopedia
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(New page: 200px<br /><applet load="1lr1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lr1" /> '''Solution Structure of the Oligomerization Do...)
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Revision as of 18:40, 20 November 2007
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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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