1bi1
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1bi1.gif|left|200px]] | [[Image:1bi1.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1bi1", 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_1bi1| PDB=1bi1 | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''STRUCTURE OF APO-AND HOLO-DIPHTHERIA TOXIN REPRESSOR''' | '''STRUCTURE OF APO-AND HOLO-DIPHTHERIA TOXIN REPRESSOR''' | ||
| Line 27: | Line 24: | ||
[[Category: Hol, W G.J.]] | [[Category: Hol, W G.J.]] | ||
[[Category: Pohl, E.]] | [[Category: Pohl, E.]] | ||
| - | [[Category: | + | [[Category: Dna-binding]] |
| - | [[Category: | + | [[Category: Iron]] |
| - | [[Category: | + | [[Category: Repressor]] |
| - | [[Category: | + | [[Category: Transcription regulation]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:32:22 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 08:32, 2 May 2008
STRUCTURE OF APO-AND HOLO-DIPHTHERIA TOXIN REPRESSOR
Overview
The diphtheria toxin repressor (DtxR) from Corynebacterium diphtheriae is a divalent metal-activated repressor of chromosomal genes that encode proteins responsible for siderophore-mediated iron uptake and also of the gene of certain corynebacteriophages that encodes diphtheria toxin. DtxR consists of two 25.3-kDa three-domain subunits and is a member of a family of related repressor proteins in several Gram-positive bacterial species, some of which are important human pathogens. In this paper, we report on the first high resolution crystal structures of apo-DtxR in two related space groups. In addition, crystal structures of Zn-DtxR were determined in the same two space groups. The resolutions of the structures range from 2.2 to 2.4 A. The four refined models of the apo- and the holo-repressor exhibit quite similar metal binding centers, which do, however, show higher thermal motion in the apo-structures. All four structures reported differ from each other in one important aspect. The N-terminal DNA-binding domain and the last 20 residues of the dimerization domain of each subunit move significantly with respect to the core of the DtxR dimer, which consists of residues 74-120 from both subunits. These results provide the first indication of a conformational change that may occur upon binding of the holo-repressor to DNA.
About this Structure
1BI1 is a Single protein structure of sequence from Corynebacterium diphtheriae. Full crystallographic information is available from OCA.
Reference
Motion of the DNA-binding domain with respect to the core of the diphtheria toxin repressor (DtxR) revealed in the crystal structures of apo- and holo-DtxR., Pohl E, Holmes RK, Hol WG, J Biol Chem. 1998 Aug 28;273(35):22420-7. PMID:9712865 Page seeded by OCA on Fri May 2 11:32:22 2008
