6v7l: Difference between revisions
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The | ==The structure of the P212121 crystal form of canavalin at 173 K== | ||
<StructureSection load='6v7l' size='340' side='right'caption='[[6v7l]], [[Resolution|resolution]] 2.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6v7l]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6V7L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6V7L FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BEZ:BENZOIC+ACID'>BEZ</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=6v7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v7l OCA], [http://pdbe.org/6v7l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6v7l RCSB], [http://www.ebi.ac.uk/pdbsum/6v7l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6v7l ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/CANA_CANEN CANA_CANEN]] Seed storage protein. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
X-ray intensities extending to 1.4 A resolution were collected on the P63 hexagonal crystal form of canavalin, and extended to 1.9 A for the orthorhombic C2221 crystals. Structure determination of a new crystal form of canavalin having space group P212121 is reported as well. Both the N and C terminal cupin domains contained identifiable ligands. For hexagonal crystals, in the cavity of the C terminal cupin, a molecule of benzoic acid was found, bound through carboxyl oxygens to Histidine 297, asparagine 284 and Arginine 376. The benzene ring was immersed in a cluster of at least 8 hydrophobic amino acid side chains. The N terminal cupin contained a molecule of citrate. Benzoic acid was also found to be present in the C terminal cupins of in the C2221 and P212121 crystal forms. In rhombohedral crystals, the C terminal cupin domain appeared to be occupied by a phosphate ion, but this was ambiguous. In cubic crystals, both domains were vacant. The N terminal cupin domains of canavalin in the P212121 and rhombohedral crystals were also vacant, but the N terminal cupin domain of the C2221 crystals contained a ligand whose identity is uncertain, but which has been modeled as HEPES buffer. A possible physiological role for the ligands and their complexes with canavalin is considered. | |||
Binding of benzoic acid and anions within the cupin domains of the vicilin protein canavalin from jack bean (Canavalia ensiformis): Crystal structures.,McPherson A Biochem Biophys Res Commun. 2020 Jan 23. pii: S0006-291X(20)30176-5. doi:, 10.1016/j.bbrc.2020.01.101. PMID:31983433<ref>PMID:31983433</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6v7l" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: McPherson, A]] | |||
[[Category: Benzoic acid]] | |||
[[Category: Plant protein]] | |||
[[Category: Precanavalin]] | |||
[[Category: Proteolytic cleavage]] | |||
[[Category: Storage protein]] | |||
[[Category: Vicillim]] | |||
