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1lr1
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= hns ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= hns ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1hns|1HNS]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lr1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lr1 OCA], [http://www.ebi.ac.uk/pdbsum/1lr1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lr1 RCSB]</span> | ||
}} | }} | ||
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[[Category: nucleoid assembly]] | [[Category: nucleoid assembly]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:06:16 2008'' |
Revision as of 19:06, 30 March 2008
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| Gene: | hns (Escherichia coli) | ||||||
| Related: | 1HNS
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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