1lr1
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1lr1.gif|left|200px]] | [[Image:1lr1.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1lr1", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_1lr1| PDB=1lr1 | SCENE= }} | |
| - | + | ||
| - | | | + | |
| - | }} | + | |
'''Solution Structure of the Oligomerization Domain of the Bacterial Chromatin-Structuring Protein H-NS''' | '''Solution Structure of the Oligomerization Domain of the Bacterial Chromatin-Structuring Protein H-NS''' | ||
| Line 36: | Line 33: | ||
[[Category: Ono, S.]] | [[Category: Ono, S.]] | ||
[[Category: Petrovic, A.]] | [[Category: Petrovic, A.]] | ||
| - | [[Category: | + | [[Category: Chromatin]] |
| - | [[Category: | + | [[Category: Coiled-coil]] |
| - | [[Category: | + | [[Category: Dna packaging]] |
| - | [[Category: | + | [[Category: Nucleoid assembly]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:12:02 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 21:12, 2 May 2008
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 Sat May 3 00:12:02 2008
