6QUG

GHK tagged MBP-Nup98(1-29)

Summary for 6QUG

• Entry DOI: 10.2210/pdb6qug/pdb
• Related: 6QUH 6QUI 6QUJ
• Descriptor: Maltodextrin-binding protein,Nucleoporin, putative, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, COPPER (II) ION, ... (6 entities in total)
• Functional Keywords: mbp fusion nup98, transport protein
• Biological source: Escherichia coli; More
• Total number of polymer chains: 12
• Total formula weight: 525748.50

Authors

Huyton, T.,Gorlich, D. (deposition date: 2019-02-27, release date: 2020-05-27, Last modification date: 2024-05-15)

Primary citation

Mehr, A.,Henneberg, F.,Chari, A.,Gorlich, D.,Huyton, T.
The copper(II)-binding tripeptide GHK, a valuable crystallization and phasing tag for macromolecular crystallography.
Acta Crystallogr D Struct Biol, 76:1222-1232, 2020

PubMed Abstract: The growth of diffraction-quality crystals and experimental phasing remain two of the main bottlenecks in protein crystallography. Here, the high-affinity copper(II)-binding tripeptide GHK was fused to the N-terminus of a GFP variant and an MBP-FG peptide fusion. The GHK tag promoted crystallization, with various residues (His, Asp, His/Pro) from symmetry molecules completing the copper(II) square-pyramidal coordination sphere. Rapid structure determination by copper SAD phasing could be achieved, even at a very low Bijvoet ratio or after significant radiation damage. When collecting highly redundant data at a wavelength close to the copper absorption edge, residual S-atom positions could also be located in log-likelihood-gradient maps and used to improve the phases. The GHK copper SAD method provides a convenient way of both crystallizing and phasing macromolecular structures, and will complement the current trend towards native sulfur SAD and MR-SAD phasing.

PubMed: 33263328
DOI: 10.1107/S2059798320013741

Experimental method

X-RAY DIFFRACTION (2.7 Å)