7mg7: Difference between revisions
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==== | ==Concanavalin A bound to a DNA glycoconjugate, Man-GTAC== | ||
<StructureSection load='7mg7' size='340' side='right'caption='[[7mg7]]' scene=''> | <StructureSection load='7mg7' size='340' side='right'caption='[[7mg7]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | <table><tr><td colspan='2'>[[7mg7]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7MG7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MG7 FirstGlance]. <br> | ||
</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=7mg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7mg7 OCA], [https://pdbe.org/7mg7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7mg7 RCSB], [https://www.ebi.ac.uk/pdbsum/7mg7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7mg7 ProSAT]</span></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]] 1.75Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SQ0:3-{[2-(2-hydroxyethoxy)ethyl]amino}-4-[(6-hydroxyhexyl)amino]cyclobut-3-ene-1,2-dione'>SQ0</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=7mg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7mg7 OCA], [https://pdbe.org/7mg7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7mg7 RCSB], [https://www.ebi.ac.uk/pdbsum/7mg7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7mg7 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/CONA_CANEN CONA_CANEN] D-mannose specific lectin. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Proteins are exquisite nanoscale building blocks: molecularly pure, chemically addressable, and inherently selective for their evolved function. The organization of proteins into single crystals with high positional, orientational, and translational order results in materials where the location of every atom can be known. However, controlling the organization of proteins is challenging due to the myriad interactions that define protein interfaces within native single crystals. Recently, we discovered that introducing a single DNA-DNA interaction between protein surfaces leads to changes in the packing of proteins within single crystals and the protein-protein interactions (PPIs) that arise. However, modifying specific PPIs to effect deliberate changes to protein packing is an unmet challenge. In this work, we hypothesized that disrupting and replacing a highly conserved PPI with a DNA-DNA interaction would enable protein packing to be modulated by exploiting the programmability of the introduced oligonucleotides. Using concanavalin A (ConA) as a model protein, we circumvent potentially deleterious mutagenesis and exploit the selective binding of ConA toward mannose to noncovalently attach DNA to the protein surface. We show that DNA association eliminates the major PPI responsible for crystallization of native ConA, thereby allowing subtle changes to DNA design (length, complementarity, and attachment position) to program distinct changes to ConA packing, including the realization of three novel crystal structures and the deliberate expansion of ConA packing along a single crystallographic axis. These findings significantly enhance our understanding of how DNA can supersede native PPIs to program protein packing within ordered materials. | |||
Redefining Protein Interfaces within Protein Single Crystals with DNA.,Partridge BE, Winegar PH, Han Z, Mirkin CA J Am Chem Soc. 2021 Jun 16;143(23):8925-8934. doi: 10.1021/jacs.1c04191. Epub, 2021 Jun 5. PMID:34096291<ref>PMID:34096291</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7mg7" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Concanavalin 3D structures|Concanavalin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Canavalia ensiformis]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Synthetic construct]] | ||
[[Category: Mirkin CA]] | |||
[[Category: Partridge BE]] | |||
[[Category: Winegar PH]] | |||