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[[Image:1xdt.gif|left|200px]]
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{{STRUCTURE_1xdt|  PDB=1xdt  |  SCENE=  }}
'''COMPLEX OF DIPHTHERIA TOXIN AND HEPARIN-BINDING EPIDERMAL GROWTH FACTOR'''


==COMPLEX OF DIPHTHERIA TOXIN AND HEPARIN-BINDING EPIDERMAL GROWTH FACTOR==
<StructureSection load='1xdt' size='340' side='right'caption='[[1xdt]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1xdt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_diphtheriae Corynebacterium diphtheriae] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XDT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XDT FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.65&#8491;</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=1xdt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xdt OCA], [https://pdbe.org/1xdt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xdt RCSB], [https://www.ebi.ac.uk/pdbsum/1xdt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xdt 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>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xd/1xdt_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1xdt ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We describe the crystal structure at 2.65 A resolution of diphtheria toxin (DT) complexed 1:1 with a fragment of its cell-surface receptor, the precursor of heparin-binding epidermal-growth-factor-like growth factor (HBEGF). HBEGF in the complex has the typical EGF-like fold and packs its principal beta hairpin against the face of a beta sheet in the receptor-binding domain of DT. The interface has a predominantly hydrophobic core, and polar interactions are formed at the periphery. The structure of the complex suggests that part of the membrane anchor of the receptor can interact with a hinge region of DT. The toxin molecule is thereby induced to form an open conformation conducive to membrane insertion. The structure provides a basis for altering the binding specificity of the toxin, and may also serve as a model for other EGF-receptor interactions.


==Overview==
Crystal structure of the complex of diphtheria toxin with an extracellular fragment of its receptor.,Louie GV, Yang W, Bowman ME, Choe S Mol Cell. 1997 Dec;1(1):67-78. PMID:9659904<ref>PMID:9659904</ref>
We describe the crystal structure at 2.65 A resolution of diphtheria toxin (DT) complexed 1:1 with a fragment of its cell-surface receptor, the precursor of heparin-binding epidermal-growth-factor-like growth factor (HBEGF). HBEGF in the complex has the typical EGF-like fold and packs its principal beta hairpin against the face of a beta sheet in the receptor-binding domain of DT. The interface has a predominantly hydrophobic core, and polar interactions are formed at the periphery. The structure of the complex suggests that part of the membrane anchor of the receptor can interact with a hinge region of DT. The toxin molecule is thereby induced to form an open conformation conducive to membrane insertion. The structure provides a basis for altering the binding specificity of the toxin, and may also serve as a model for other EGF-receptor interactions.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1XDT is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Corynebacterium_diphtheriae Corynebacterium diphtheriae] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XDT OCA].
</div>
<div class="pdbe-citations 1xdt" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Crystal structure of the complex of diphtheria toxin with an extracellular fragment of its receptor., Louie GV, Yang W, Bowman ME, Choe S, Mol Cell. 1997 Dec;1(1):67-78. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9659904 9659904]
*[[Diphtheria toxin|Diphtheria toxin]]
*[[Epidermal growth factor|Epidermal growth factor]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Corynebacterium diphtheriae]]
[[Category: Corynebacterium diphtheriae]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Bowman, M E.]]
[[Category: Bowman ME]]
[[Category: Choe, S.]]
[[Category: Choe S]]
[[Category: Louie, G V.]]
[[Category: Louie GV]]
[[Category: Yang, W.]]
[[Category: Yang W]]
[[Category: Diphtheria toxin]]
[[Category: Epidermal growth factor]]
[[Category: Heparin-binding epidermal growth factor]]
[[Category: Receptor]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 14:53:59 2008''