7mga

Concanavalin A bound to a DNA glycoconjugate, Man-AAATTT

spinqualitylabelsall models 7mga, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7mga is a 4 chain structure with sequence from Canavalia ensiformis and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: CA, MAN, MN, SQ0 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CONA_CANEN D-mannose specific lectin. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Concanavalin 3D structures

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