6lng

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Rapid crystallization of streptavidin using charged peptidesRapid crystallization of streptavidin using charged peptides

Structural highlights

6lng is a 6 chain structure with sequence from Streptomyces avidinii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8000015Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SAV_STRAV The biological function of streptavidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin).

Publication Abstract from PubMed

We utilized electrostatic interaction to induce rapid crystallization of streptavidin. Simply mixing streptavidins possessing either a positively or negatively charged peptide at their C-terminus generated diffraction-quality crystals in a few hours. We modified the streptavidin crystals with fluorescent molecules using biotin, demonstrating the concept of protein crystals as functional biomaterials.

Genetically fused charged peptides induce rapid crystallization of proteins.,Minamihata K, Tsukamoto K, Adachi M, Shimizu R, Mishina M, Kuroki R, Nagamune T Chem Commun (Camb). 2020 Mar 5. doi: 10.1039/c9cc09529b. PMID:32134050[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Minamihata K, Tsukamoto K, Adachi M, Shimizu R, Mishina M, Kuroki R, Nagamune T. Genetically fused charged peptides induce rapid crystallization of proteins. Chem Commun (Camb). 2020 Mar 5. doi: 10.1039/c9cc09529b. PMID:32134050 doi:http://dx.doi.org/10.1039/c9cc09529b

6lng, resolution 1.80Å

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OCA