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1lr1
From Proteopedia
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| - | [[Image:1lr1.gif|left|200px]] | + | [[Image:1lr1.gif|left|200px]] |
| - | + | ||
| - | '''Solution Structure of the Oligomerization Domain of the Bacterial Chromatin-Structuring Protein H-NS''' | + | {{Structure |
| + | |PDB= 1lr1 |SIZE=350|CAPTION= <scene name='initialview01'>1lr1</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= hns ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''Solution Structure of the Oligomerization Domain of the Bacterial Chromatin-Structuring Protein H-NS''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1LR1 is a [ | + | 1LR1 is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12460581 12460581] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 29: | Line 38: | ||
[[Category: nucleoid assembly]] | [[Category: nucleoid assembly]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:34:08 2008'' |
Revision as of 10:34, 20 March 2008
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| Gene: | hns (Escherichia coli) | ||||||
| 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
Page seeded by OCA on Thu Mar 20 12:34:08 2008
