2GBJ

Crystal Structure of the 9-10 8 Glycine Insertion Mutant of Ubiquitin.

Summary for 2GBJ

• Entry DOI: 10.2210/pdb2gbj/pdb
• Related: 2GBK 2GBM 2GBN 2GBR
• Descriptor: Ubiquitin (2 entities in total)
• Functional Keywords: loop insertion, protein binding
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 18066.49

Authors

Ferraro, D.M.,Ferraro, D.J.,Ramaswamy, S.,Robertson, A.D. (deposition date: 2006-03-10, release date: 2006-05-16, Last modification date: 2023-08-30)

Primary citation

Ferraro, D.M.,Ferraro, D.J.,Ramaswamy, S.,Robertson, A.D.
Structures of Ubiquitin Insertion Mutants Support Site-specific Reflex Response to Insertions Hypothesis.
J.Mol.Biol., 359:390-402, 2006

PubMed Abstract: We previously concluded that, judging from NMR chemical shifts, the effects of insertions into ubiquitin on its conformation appear to depend primarily on the site of insertion rather than the sequence of the insertion. To obtain a more complete and atomic-resolution understanding of how these insertions modulate the conformation of ubiquitin, we have solved the crystal structures of four insertional mutants of ubiquitin. Insertions between residues 9 and 10 of ubiquitin are minimally perturbing to the remainder of the protein, while larger alterations occur when the insertion is between residues 35 and 36. Further, the alterations in response to insertions are very similar for each mutant at a given site. Two insertions, one at each site, were designed from structurally homologous proteins. Interestingly, the secondary structure within these five to seven amino acid residue insertions is conserved in the new protein. Overall, the crystal structures support the previous conclusion that the conformational effects of these insertions are determined largely by the site of insertion and only secondarily by the sequence of the insert.

PubMed: 16647719
DOI: 10.1016/j.jmb.2006.03.047

Experimental method

X-RAY DIFFRACTION (1.35 Å)