1mu4
From Proteopedia
(New page: 200px<br /><applet load="1mu4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mu4, resolution 1.80Å" /> '''CRYSTAL STRUCTURE AT...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1mu4.jpg|left|200px]]<br /><applet load="1mu4" size=" | + | [[Image:1mu4.jpg|left|200px]]<br /><applet load="1mu4" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mu4, resolution 1.80Å" /> | caption="1mu4, resolution 1.80Å" /> | ||
'''CRYSTAL STRUCTURE AT 1.8 ANGSTROMS OF THE BACILLUS SUBTILIS CATABOLITE REPRESSION HISTIDINE CONTAINING PROTEIN (CRH)'''<br /> | '''CRYSTAL STRUCTURE AT 1.8 ANGSTROMS OF THE BACILLUS SUBTILIS CATABOLITE REPRESSION HISTIDINE CONTAINING PROTEIN (CRH)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the regulatory protein Crh from Bacillus subtilis | + | The crystal structure of the regulatory protein Crh from Bacillus subtilis was solved at 1.8A resolution and showed an intertwined dimer formed by N-terminal beta1-strand swapping of two monomers. Comparison with the monomeric NMR structure of Crh revealed a domain swap induced conformational rearrangement of the putative interaction site with the repressor CcpA. The resulting conformation closely resembles that observed for the monomeric Crh homologue HPr, indicating that the Crh dimer is the active form binding to CcpA. An analogous dimer of HPr can be constructed without domain swapping, suggesting that HPr may dimerize upon binding to CcpA. Our data suggest that reversible 3D domain swapping of Crh might be an efficient regulatory mechanism to modulate its activity. |
==About this Structure== | ==About this Structure== | ||
| - | 1MU4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1MU4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MU4 OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Haser, R.]] | [[Category: Haser, R.]] | ||
| - | [[Category: Juy, M | + | [[Category: Juy, M R.]] |
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: open-faced b-sandwich]] | [[Category: open-faced b-sandwich]] | ||
| Line 20: | Line 20: | ||
[[Category: swapping domain]] | [[Category: swapping domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:59:04 2008'' |
Revision as of 11:59, 21 February 2008
|
CRYSTAL STRUCTURE AT 1.8 ANGSTROMS OF THE BACILLUS SUBTILIS CATABOLITE REPRESSION HISTIDINE CONTAINING PROTEIN (CRH)
Overview
The crystal structure of the regulatory protein Crh from Bacillus subtilis was solved at 1.8A resolution and showed an intertwined dimer formed by N-terminal beta1-strand swapping of two monomers. Comparison with the monomeric NMR structure of Crh revealed a domain swap induced conformational rearrangement of the putative interaction site with the repressor CcpA. The resulting conformation closely resembles that observed for the monomeric Crh homologue HPr, indicating that the Crh dimer is the active form binding to CcpA. An analogous dimer of HPr can be constructed without domain swapping, suggesting that HPr may dimerize upon binding to CcpA. Our data suggest that reversible 3D domain swapping of Crh might be an efficient regulatory mechanism to modulate its activity.
About this Structure
1MU4 is a Single protein structure of sequence from Bacillus subtilis with as ligand. Full crystallographic information is available from OCA.
Reference
Dimerization of Crh by reversible 3D domain swapping induces structural adjustments to its monomeric homologue Hpr., Juy M, Penin F, Favier A, Galinier A, Montserret R, Haser R, Deutscher J, Bockmann A, J Mol Biol. 2003 Sep 26;332(4):767-76. PMID:12972249
Page seeded by OCA on Thu Feb 21 13:59:04 2008
