3px8: Difference between revisions

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==RTA in complex with 7-carboxy-pterin==
==RTA in complex with 7-carboxy-pterin==
<StructureSection load='3px8' size='340' side='right' caption='[[3px8]], [[Resolution|resolution]] 1.29&Aring;' scene=''>
<StructureSection load='3px8' size='340' side='right'caption='[[3px8]], [[Resolution|resolution]] 1.29&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3px8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Castor_bean Castor bean]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PX8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PX8 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3px8]] 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=3PX8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PX8 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=JP2:2-AMINO-4-OXO-1,4-DIHYDROPTERIDINE-7-CARBOXYLIC+ACID'>JP2</scene></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]] 1.29&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3px9|3px9]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=JP2:2-AMINO-4-OXO-1,4-DIHYDROPTERIDINE-7-CARBOXYLIC+ACID'>JP2</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3px8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3px8 OCA], [http://pdbe.org/3px8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3px8 RCSB], [http://www.ebi.ac.uk/pdbsum/3px8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3px8 ProSAT]</span></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=3px8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3px8 OCA], [https://pdbe.org/3px8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3px8 RCSB], [https://www.ebi.ac.uk/pdbsum/3px8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3px8 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[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).
Ricin is a potent toxin found in castor seeds. The A chain, RTA, enzymaticlly depurinates a specific adenosine in ribosomal RNA, inhibiting protein synthesis. Ricin is a known chemical weapons threat having no effective antidote. This makes the discovery of new inhibitors of great importance. We have previously used 6-substituted pterins, such as pteroic acid, as an inhibitor platform with moderate success. We now report the success of 7-carboxy pterin (7CP) as an RTA inhibitor; its binding has been monitored using both kinetic and temperature shift assays and by X-ray crystallography. We also discuss the synthesis of various derivatives of 7CP, and their binding affinity and inhibitory effects, as part of a program to make effective RTA inhibitors.
 
7-Substituted pterins provide a new direction for ricin A chain inhibitors.,Pruet JM, Jasheway KR, Manzano LA, Bai Y, Anslyn EV, Robertus JD Eur J Med Chem. 2011 May 20. PMID:21641093<ref>PMID:21641093</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3px8" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Ricin|Ricin]]
*[[Ricin 3D structures|Ricin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Castor bean]]
[[Category: Large Structures]]
[[Category: Jasheway, K R]]
[[Category: Ricinus communis]]
[[Category: Robertus, J D]]
[[Category: Jasheway KR]]
[[Category: Hydrolase]]
[[Category: Robertus JD]]
[[Category: Hydrolase-inhibitor complex]]
[[Category: N-glycosidase]]
[[Category: Protein-ligand complex]]
[[Category: Pterin]]
[[Category: Ribosome inactivating protein]]
[[Category: Ricin]]
[[Category: Toxin]]

Latest revision as of 13:44, 21 February 2024

RTA in complex with 7-carboxy-pterinRTA in complex with 7-carboxy-pterin

Structural highlights

3px8 is a 1 chain structure with sequence from Ricinus communis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.29Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).

See Also

3px8, resolution 1.29Å

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