5ebx

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[[Image:5ebx.png|left|200px]]
 
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==THE CRYSTAL STRUCTURE OF ERABUTOXIN A AT 2.0 ANGSTROMS RESOLUTION==
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The line below this paragraph, containing "STRUCTURE_5ebx", creates the "Structure Box" on the page.
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<StructureSection load='5ebx' size='340' side='right'caption='[[5ebx]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[5ebx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Laticauda_semifasciata Laticauda semifasciata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EBX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EBX 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&#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=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_5ebx| PDB=5ebx | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ebx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ebx OCA], [https://pdbe.org/5ebx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ebx RCSB], [https://www.ebi.ac.uk/pdbsum/5ebx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ebx ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/3S1EA_LATSE 3S1EA_LATSE] Binds with high affinity to muscular nicotinic acetylcholine receptors (nAChRs) (tested on Torpedo marmorata, Kd=21 uM) and with low affinity to neuronal alpha-7/CHRNA7 nAChRs (tested on chimeric alpha-7/CHRNA7, Kd=0.07 nM) and inhibits acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission (PubMed:7721859). Blocks the extracellular increase of dopamine evoked by nicotine at 4.2 uM concentrations (PubMed:9840221). In vivo, produces peripheral paralysis.<ref>PMID:7721859</ref> <ref>PMID:9305882</ref> <ref>PMID:9840221</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eb/5ebx_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=5ebx ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The three-dimensional structure of erabutoxin a, a single-chain, 62-residue protein neurotoxin from snake venom, has been determined to 2.0-A resolution by x-ray crystal structure analysis. Molecular replacement methods were used, and the structure refined to a residual R = 0.17. The sites of 62 water molecules and 1 sulfate ion have been located and refined. The structure of erabutoxin a is very similar to that established earlier for erabutoxin b. These toxins from venom of the same snake differ in sequence only at residue 26, which is Asn in erabutoxin a and His in erabutoxin b. The substitution leads to only minor variations in intramolecular hydrogen bonding. Furthermore, the distribution of thermal parameters and the implied regional mobilities are similar in the two structures. In particular, the highly mobile character of the peripheral segment Pro44-Gly49 in both structures supports the specific role proposed for this segment in neurotoxin binding to the acetylcholine receptor. Forty-eight of the solvent sites determined are first surface positions; approximately one-half of these are equivalent to solvent sites in erabutoxin b.
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===THE CRYSTAL STRUCTURE OF ERABUTOXIN A AT 2.0 ANGSTROMS RESOLUTION===
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The crystal structure of erabutoxin a at 2.0-A resolution.,Corfield PW, Lee TJ, Low BW J Biol Chem. 1989 Jun 5;264(16):9239-42. PMID:2722828<ref>PMID:2722828</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5ebx" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 2722828 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_2722828}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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[[5ebx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Laticauda_semifasciata Laticauda semifasciata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EBX OCA].
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==Reference==
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<ref group="xtra">PMID:002722828</ref><references group="xtra"/>
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[[Category: Laticauda semifasciata]]
[[Category: Laticauda semifasciata]]
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[[Category: Corfield, P W.R.]]
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[[Category: Corfield PWR]]
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[[Category: Lee, T J.]]
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[[Category: Lee T-J]]
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[[Category: Low, B W.]]
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[[Category: Low BW]]
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[[Category: Toxin]]
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Current revision

THE CRYSTAL STRUCTURE OF ERABUTOXIN A AT 2.0 ANGSTROMS RESOLUTION

PDB ID 5ebx

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