1dtp: Difference between revisions

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[[Image:1dtp.png|left|200px]]


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==THE STRUCTURE OF THE ISOLATED CATALYTIC DOMAIN OF DIPHTHERIA TOXIN==
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<StructureSection load='1dtp' size='340' side='right'caption='[[1dtp]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1dtp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynephage_beta Corynephage beta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DTP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DTP FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=APU:ADENYLYL-3-5-PHOSPHO-URIDINE-3-MONOPHOSPHATE'>APU</scene></td></tr>
{{STRUCTURE_1dtp|  PDB=1dtp  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dtp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dtp OCA], [https://pdbe.org/1dtp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dtp RCSB], [https://www.ebi.ac.uk/pdbsum/1dtp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dtp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DTX_CORBE DTX_CORBE] Diphtheria toxin, produced by a phage infecting Corynebacterium diphtheriae, is a proenzyme that, after activation, catalyzes the covalent attachment of the ADP ribose moiety of NAD to eukaryotic elongation factor 2 (eEF-2). Fragment A is the catalytic portion responsible for enzymatic ADP-ribosylation of elongation factor 2, while fragment B is responsible for binding of toxin to cell receptors and entry of fragment A.<ref>PMID:18276581</ref> <ref>PMID:19793133</ref>  


===THE STRUCTURE OF THE ISOLATED CATALYTIC DOMAIN OF DIPHTHERIA TOXIN===
==See Also==
 
*[[Diphtheria toxin|Diphtheria toxin]]
 
== References ==
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{{ABSTRACT_PUBMED_7827036}}
 
==About this Structure==
1DTP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Corynephage_beta Corynephage beta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DTP OCA].
 
==Reference==
Structure of the isolated catalytic domain of diphtheria toxin., Weiss MS, Blanke SR, Collier RJ, Eisenberg D, Biochemistry. 1995 Jan 24;34(3):773-81. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7827036 7827036]
[[Category: Corynephage beta]]
[[Category: Corynephage beta]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Eisenberg, D.]]
[[Category: Eisenberg D]]
[[Category: Weiss, M S.]]
[[Category: Weiss MS]]
[[Category: Toxin]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:36:09 2008''

Latest revision as of 09:59, 7 February 2024

THE STRUCTURE OF THE ISOLATED CATALYTIC DOMAIN OF DIPHTHERIA TOXINTHE STRUCTURE OF THE ISOLATED CATALYTIC DOMAIN OF DIPHTHERIA TOXIN

Structural highlights

1dtp is a 1 chain structure with sequence from Corynephage beta. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DTX_CORBE Diphtheria toxin, produced by a phage infecting Corynebacterium diphtheriae, is a proenzyme that, after activation, catalyzes the covalent attachment of the ADP ribose moiety of NAD to eukaryotic elongation factor 2 (eEF-2). Fragment A is the catalytic portion responsible for enzymatic ADP-ribosylation of elongation factor 2, while fragment B is responsible for binding of toxin to cell receptors and entry of fragment A.[1] [2]

See Also

References

  1. ↑ Jorgensen R, Purdy AE, Fieldhouse RJ, Kimber MS, Bartlett DH, Rod Merrill A. Cholix toxin, a novel ADP-ribosylating factor from vibrio cholerae. J Biol Chem. 2008 Feb 25;. PMID:18276581 doi:M710008200
  2. ↑ Turgeon Z, White D, Jorgensen R, Visschedyk D, Fieldhouse RJ, Mangroo D, Merrill AR. Yeast as a tool for characterizing mono-ADP-ribosyltransferase toxins. FEMS Microbiol Lett. 2009 Nov;300(1):97-106. Epub 2009 Aug 31. PMID:19793133 doi:10.1111/j.1574-6968.2009.01777.x

1dtp, resolution 2.50Å

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