2MSG

Solid-state NMR structure of ubiquitin

Summary for 2MSG

• Entry DOI: 10.2210/pdb2msg/pdb
• Related: 1D3Z 3ONS
• NMR Information: BMRB: 25123
• Descriptor: Ubiquitin (1 entity in total)
• Functional Keywords: ubiquitin fold, signaling protein
• Biological source: Homo sapiens (human)
• Cellular location: Ubiquitin: Cytoplasm : P0CG47
• Total number of polymer chains: 1
• Total formula weight: 8192.38

Authors

Lakomek, N.,Habenstein, B.,Loquet, A.,Shi, C.,Giller, K.,Wolff, S.,Becker, S.,Fasshuber, H.,Lange, A. (deposition date: 2014-08-04, release date: 2015-02-18, Last modification date: 2024-05-15)

Primary citation

Fasshuber, H.K.,Lakomek, N.A.,Habenstein, B.,Loquet, A.,Shi, C.,Giller, K.,Wolff, S.,Becker, S.,Lange, A.
Structural heterogeneity in microcrystalline ubiquitin studied by solid-state NMR.
Protein Sci., 24:592-598, 2015

PubMed Abstract: By applying [1-(13) C]- and [2-(13) C]-glucose labeling schemes to the folded globular protein ubiquitin, a strong reduction of spectral crowding and increase in resolution in solid-state NMR (ssNMR) spectra could be achieved. This allowed spectral resonance assignment in a straightforward manner and the collection of a wealth of long-range distance information. A high precision solid-state NMR structure of microcrystalline ubiquitin was calculated with a backbone rmsd of 1.57 to the X-ray structure and 1.32 Å to the solution NMR structure. Interestingly, we can resolve structural heterogeneity as the presence of three slightly different conformations. Structural heterogeneity is most significant for the loop region β1-β2 but also for β-strands β1, β2, β3, and β5 as well as for the loop connecting α1 and β3. This structural polymorphism observed in the solid-state NMR spectra coincides with regions that showed dynamics in solution NMR experiments on different timescales.

PubMed: 25644665
DOI: 10.1002/pro.2654

Experimental method

SOLID-STATE NMR