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1bi3

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Revision as of 10:57, 8 November 2017

STRUCTURE OF APO-AND HOLO-DIPHTHERIA TOXIN REPRESSOR

Structural highlights

1bi3 is a 2 chain structure with sequence from "bacillus_diphtheriae"_kruse_in_flugge_1886 "bacillus diphtheriae" kruse in flugge 1886. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
NonStd Res:
Gene:	DTXR ("Bacillus diphtheriae" Kruse in Flugge 1886)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[DTXR_CORDI] Iron-binding repressor of the dipheteria toxin gene expression. May serve as a global regulator of gene expression. Represses ripA under iron excess.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Pohl E, Holmes RK, Hol WG. 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. J Biol Chem. 1998 Aug 28;273(35):22420-7. PMID:9712865

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1bi3"

@@ Line 1: / Line 1: @@
 ==STRUCTURE OF APO-AND HOLO-DIPHTHERIA TOXIN REPRESSOR==
 <StructureSection load='1bi3' size='340' side='right' caption='[[1bi3]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DTXR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1717 "Bacillus diphtheriae" Kruse in Flugge 1886])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bi3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bi3 OCA], [http://pdbe.org/1bi3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bi3 RCSB], [http://www.ebi.ac.uk/pdbsum/1bi3 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bi3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bi3 OCA], [http://pdbe.org/1bi3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bi3 RCSB], [http://www.ebi.ac.uk/pdbsum/1bi3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bi3 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 29: / Line 30: @@
 </div>
 <div class="pdbe-citations 1bi3" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Diphtheria toxin repressor|Diphtheria toxin repressor]]
 == References ==
 <references/>

1bi3

From Proteopedia

Revision as of 10:57, 8 November 2017

STRUCTURE OF APO-AND HOLO-DIPHTHERIA TOXIN REPRESSOR

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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