1dpr
From Proteopedia
(Difference between revisions)
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<StructureSection load='1dpr' size='340' side='right'caption='[[1dpr]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='1dpr' size='340' side='right'caption='[[1dpr]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1dpr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1dpr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_diphtheriae Corynebacterium diphtheriae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DPR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DPR FirstGlance]. <br> |
- | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dpr OCA], [https://pdbe.org/1dpr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dpr RCSB], [https://www.ebi.ac.uk/pdbsum/1dpr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dpr ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</td></tr> |
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dpr OCA], [https://pdbe.org/1dpr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dpr RCSB], [https://www.ebi.ac.uk/pdbsum/1dpr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dpr ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
- | + | [https://www.uniprot.org/uniprot/DTXR_CORDI 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dpr ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dpr ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | The diphtheria tox repressor (DtxR) of Corynebacterium diphtheriae plays a critical role in the regulation of diphtheria toxin expression and the control of other iron-sensitive genes. The crystal structures of apo-DtxR and of the metal ion-activated form of the repressor have been solved and used to identify motifs involved in DNA and metal ion binding. Residues involved in binding of the activated repressor to the diphtheria tox operator, glutamine 43, arginine 47, and arginine 50, were located and confirmed by site-directed mutagenesis. Previous biochemical and genetic data can be explained in terms of these structures. Conformational differences between apo- and Ni-DtxR are discussed with regard to the mechanism of action of this repressor. | ||
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- | Structures of the apo- and the metal ion-activated forms of the diphtheria tox repressor from Corynebacterium diphtheriae.,Schiering N, Tao X, Zeng H, Murphy JR, Petsko GA, Ringe D Proc Natl Acad Sci U S A. 1995 Oct 10;92(21):9843-50. PMID:7568230<ref>PMID:7568230</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1dpr" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Diphtheria toxin repressor|Diphtheria toxin repressor]] | *[[Diphtheria toxin repressor|Diphtheria toxin repressor]] | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Corynebacterium diphtheriae]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Murphy | + | [[Category: Murphy J]] |
- | [[Category: Petsko | + | [[Category: Petsko GA]] |
- | [[Category: Ringe | + | [[Category: Ringe D]] |
- | [[Category: Schiering | + | [[Category: Schiering N]] |
- | [[Category: Tao | + | [[Category: Tao X]] |
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Current revision
STRUCTURES OF THE APO-AND METAL ION ACTIVATED FORMS OF THE DIPHTHERIA TOX REPRESSOR FROM CORYNEBACTERIUM DIPHTHERIAE
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