6krb
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==High resolution crystal structure of an Acylphosphatase protein cage== | |
+ | <StructureSection load='6krb' size='340' side='right'caption='[[6krb]], [[Resolution|resolution]] 2.38Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[6krb]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae_O395 Vibrio cholerae O395]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KRB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KRB 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]] 2.375Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6krb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6krb OCA], [https://pdbe.org/6krb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6krb RCSB], [https://www.ebi.ac.uk/pdbsum/6krb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6krb ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/ACYP_VIBC3 ACYP_VIBC3] | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Protein cages have recently emerged as an extraordinary drug-delivery system due to its biocompatibility, biodegradability, low toxicity, ease to manipulate and engineer. We have reported earlier the formation and architecture of a do-decameric cage-like architecture of Vibrio cholerae acylphosphatase (VcAcP) at 3.1 A. High resolution (2.4 A) crystal structure of VcAcP cage, reported here, illuminates a potential binding site for sulphate/phosphate containing drugs whereas analysis of its subunit association and interfaces indicates high potential for cage engineering. Tryptophan quenching studies indeed discloses noteworthy binding with various sulphate/phosphate containing nucleotide-based drugs and vitamin B6 (PLP) demonstrating that exterior surface of VcAcP protein cage can be exploited as multifunctional carrier. Moreover, a quadruple mutant L30C/T68C/N40C/L81C-VcAcP (QM-VcAcP) capable to form an intricate disulphide bonded VcAcP cage has been designed. SEC, SDS-PAGE analysis and DLS experiment confirmed cysteine mediated engineered VcAcP cage formation. | ||
- | + | High resolution structure of Vibrio cholerae acylphosphatase (VcAcP) cage: Identification of drugs, location of its binding site and engineering to facilitate cage formation.,Chatterjee S, Nath S, Sen U Biochem Biophys Res Commun. 2020 Mar 5;523(2):348-353. doi:, 10.1016/j.bbrc.2019.12.060. Epub 2019 Dec 19. PMID:31866010<ref>PMID:31866010</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
- | [[Category: | + | <div class="pdbe-citations 6krb" style="background-color:#fffaf0;"></div> |
- | [[Category: Chatterjee | + | == References == |
- | [[Category: Nath | + | <references/> |
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Vibrio cholerae O395]] | ||
+ | [[Category: Chatterjee S]] | ||
+ | [[Category: Nath S]] | ||
+ | [[Category: Sen U]] |
Current revision
High resolution crystal structure of an Acylphosphatase protein cage
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