1ift

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[[Image:1ift.gif|left|200px]]<br />
 
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<applet load="1ift" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ift, resolution 1.8&Aring;" />
 
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'''RICIN A-CHAIN (RECOMBINANT)'''<br />
 
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==Overview==
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==RICIN A-CHAIN (RECOMBINANT)==
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Ricin is a potent plant toxin which acts by removing a specific adenine, residue from the ribosome. The X-ray crystal structure of a new, tetragonal crystal form of the recombinant ricin A-chain diffracting to, 1.8 A resolution has been determined via molecular replacement methods and, refined to a crystallographic R-factor of 18.6%. The higher resolution, electron density allowed improvements to be made upon previously published, models, resulting in an increase in the assigned secondary structure of, the protein. The enzyme adopts the same global conformation in this, crystal form with differences in detail due only partly to crystal, packing. The active site superimposes closely with those of previously, published models but the locations of the active-site water molecules, differ in ... [[http://ispc.weizmann.ac.il/pmbin/getpm?7990130 (full description)]]
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<StructureSection load='1ift' size='340' side='right'caption='[[1ift]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ift]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ricinus_communis Ricinus communis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IFT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IFT 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]] 1.8&#8491;</td></tr>
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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=1ift FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ift OCA], [https://pdbe.org/1ift PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ift RCSB], [https://www.ebi.ac.uk/pdbsum/1ift PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ift ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RICI_RICCO RICI_RICCO] Ricin is highly toxic to animal cells and to a lesser extent to plant cells. The A chain acts as a glycosidase that removes a specific adenine residue from an exposed loop of the 28S rRNA (A4324 in mammals), leading to rRNA breakage. As this loop is involved in elongation factor binding, modified ribosomes are catalytically inactive and unable to support protein synthesis. The A chain can inactivate a few thousand ribosomes per minute, faster than the cell can make new ones. Therefore a single A chain molecule can kill an animal cell. The B chain binds to beta-D-galactopyranoside moieties on cell surface glycoproteins and glycolipids and facilitates the entry into the cell of the A chain; B chains are also responsible for cell agglutination (Lectin activity).
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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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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/if/1ift_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1ift ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1IFT is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Ricinus_communis Ricinus communis]]. Active as [[http://en.wikipedia.org/wiki/rRNA_N-glycosylase rRNA N-glycosylase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.22 3.2.2.22]]. Structure known Active Site: ACT. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IFT OCA]].
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*[[Ricin 3D structures|Ricin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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X-ray structure of recombinant ricin A-chain at 1.8 A resolution., Weston SA, Tucker AD, Thatcher DR, Derbyshire DJ, Pauptit RA, J Mol Biol. 1994 Dec 9;244(4):410-22. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7990130 7990130]
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[[Category: Large Structures]]
[[Category: Ricinus communis]]
[[Category: Ricinus communis]]
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[[Category: Single protein]]
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[[Category: Derbyshire DJ]]
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[[Category: rRNA N-glycosylase]]
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[[Category: Pauptit RA]]
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[[Category: Derbyshire, D.J.]]
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[[Category: Thatcher DR]]
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[[Category: Pauptit, R.A.]]
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[[Category: Tucker AD]]
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[[Category: Thatcher, D.R.]]
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[[Category: Weston SA]]
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[[Category: Tucker, A.D.]]
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[[Category: Weston, S.A.]]
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[[Category: glycoprotein]]
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[[Category: glycosidase]]
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[[Category: hydrolase]]
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[[Category: toxin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:39:24 2007''
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Current revision

RICIN A-CHAIN (RECOMBINANT)

PDB ID 1ift

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