6lov
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==crystal structure of alpha-momorcharin in complex with xanthosine== | |
| + | <StructureSection load='6lov' size='340' side='right'caption='[[6lov]], [[Resolution|resolution]] 1.35Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6lov]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Momordica_charantia Momordica charantia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LOV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LOV 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]] 1.35Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4UO:2,3-DIHYDROXANTHOSINE'>4UO</scene></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=6lov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lov OCA], [https://pdbe.org/6lov PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lov RCSB], [https://www.ebi.ac.uk/pdbsum/6lov PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lov ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/RIP1_MOMCH RIP1_MOMCH] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Alpha-momorcharin (Alpha-MMC) from the seed of bitter melon is a type I ribosome inactivating protein (RIP) that removes a specific adenine from 28S rRNA and inhibits protein biosynthesis. Here, we report seven crystal complex structures of alpha-MMC with different substrate analogs (adenine, AMP, cAMP, dAMP, ADP, GMP, and xanthosine) at 1.08 A to 1.52 A resolution. These structures reveal that not only adenine, but also guanine and their analogs can effectively bind to alpha-MMC. The side chain of Tyr93 adopts two conformations, serving as a switch to open and close the substrate binding pocket of alpha-MMC. Although adenine, AMP, GMP, and guanine are located in a similar active site in different RIPs, residues involved in the interaction between RIPs and substrate analogs are slightly different. Complex structures of alpha-MMC with different substrate analogs solved in this study provide useful information on its enzymatic mechanisms and may enable the development of new inhibitors to treat the poisoning of alpha-MMC. | ||
| - | + | Atomic-resolution structures of type I ribosome inactivating protein alpha-momorcharin with different substrate analogs.,Fan X, Wang Y, Guo F, Zhang Y, Jin T Int J Biol Macromol. 2020 Dec 1;164:265-276. doi: 10.1016/j.ijbiomac.2020.07.063., Epub 2020 Jul 10. PMID:32653369<ref>PMID:32653369</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6lov" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Ribosome inactivating protein 3D structures|Ribosome inactivating protein 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Momordica charantia]] | ||
| + | [[Category: Fan X]] | ||
| + | [[Category: Jin T]] | ||
Current revision
crystal structure of alpha-momorcharin in complex with xanthosine
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