3AI4
Crystal structure of yeast enhanced green fluorescent protein - mouse polymerase iota ubiquitin binding motif fusion protein
Summary for 3AI4
| Entry DOI | 10.2210/pdb3ai4/pdb |
| Related | 3AI5 |
| Descriptor | yeast enhanced green fluorescent protein,DNA polymerase iota, SULFATE ION (3 entities in total) |
| Functional Keywords | ubm, ubiquitin-binding motif, gfp, fusion, fluorescent protein, replication |
| Biological source | Aequorea victoria (Jellyfish) More |
| Cellular location | Nucleus : Q6R3M4 |
| Total number of polymer chains | 1 |
| Total formula weight | 32186.99 |
| Authors | Suzuki, N.,Wakatsuki, S.,Kawasaki, M. (deposition date: 2010-05-10, release date: 2010-09-29, Last modification date: 2024-10-23) |
| Primary citation | Suzuki, N.,Hiraki, M.,Yamada, Y.,Matsugaki, N.,Igarashi, N.,Kato, R.,Dikic, I.,Drew, D.,Iwata, S.,Wakatsuki, S.,Kawasaki, M. Crystallization of small proteins assisted by green fluorescent protein Acta Crystallogr.,Sect.D, 66:1059-1066, 2010 Cited by PubMed Abstract: The generation of crystal lattice contacts by proteinaceous tags fused to target proteins is an attractive approach to aid in the crystallization of otherwise intractable proteins. Here, the use of green fluorescent protein (GFP) fusions for this purpose is demonstrated, using ubiquitin and the ubiquitin-binding motif (UBM) of Y-family polymerase ι as examples. The structure of the GFP-ubiquitin fusion protein revealed that the crystal lattice was formed by GFP moieties. Ubiquitin was accommodated in the lattice through interactions with the peripheral loops of GFP. However, in the GFP-UBM fusion crystal UBM formed extensive interactions with GFP and these interactions, together with UBM dimerization, mediated the crystal packing. Interestingly, the tyrosine residues that are involved in mediating crystal contacts in both GFP-ubiquitin and GFP-UBM crystals are arranged in a belt on the surface of the β-barrel structure of GFP. Therefore, it is likely that GFP can assist in the crystallization of small proteins and of protein domains in general. PubMed: 20944239DOI: 10.1107/S0907444910032944 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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