1bi0

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{{STRUCTURE_1bi0| PDB=1bi0 | SCENE= }}
{{STRUCTURE_1bi0| PDB=1bi0 | SCENE= }}
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'''STRUCTURE OF APO-AND HOLO-DIPHTHERIA TOXIN REPRESSOR'''
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===STRUCTURE OF APO-AND HOLO-DIPHTHERIA TOXIN REPRESSOR===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_9712865}}
==About this Structure==
==About this Structure==
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[[Category: Repressor]]
[[Category: Repressor]]
[[Category: Transcription regulation]]
[[Category: Transcription regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:11:52 2008''

Revision as of 16:11, 30 June 2008

Template:STRUCTURE 1bi0

STRUCTURE OF APO-AND HOLO-DIPHTHERIA TOXIN REPRESSOR

Template:ABSTRACT PUBMED 9712865

About this Structure

1BI0 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

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