2M66

Endoplasmic reticulum protein 29 (ERp29) C-terminal domain: 3D Protein Fold Determination from Backbone Amide Pseudocontact Shifts Generated by Lanthanide Tags at Multiple Sites

Summary for 2M66

• Entry DOI: 10.2210/pdb2m66/pdb
• Related: 1G7D
• NMR Information: BMRB: 4920
• Descriptor: Endoplasmic reticulum resident protein 29 (1 entity in total)
• Functional Keywords: erp29, erp29-c, chaperone, gps-rosetta
• Biological source: Rattus norvegicus (Rat)
• Cellular location: Endoplasmic reticulum lumen: P52555
• Total number of polymer chains: 1
• Total formula weight: 11787.47

Authors

Yagi, H.,Pilla, K.,Maleckis, A.,Graham, B.,Huber, T.,Otting, G. (deposition date: 2013-03-26, release date: 2013-07-10, Last modification date: 2024-05-01)

Primary citation

Yagi, H.,Pilla, K.B.,Maleckis, A.,Graham, B.,Huber, T.,Otting, G.
Three-dimensional protein fold determination from backbone amide pseudocontact shifts generated by lanthanide tags at multiple sites
Structure, 21:883-890, 2013

PubMed Abstract: Site-specific attachment of paramagnetic lanthanide ions to a protein generates pseudocontact shifts (PCS) in the nuclear magnetic resonance (NMR) spectra of the protein that are easily measured as changes in chemical shifts. By labeling the protein with lanthanide tags at four different sites, PCSs are observed for most amide protons and accurate information is obtained about their coordinates in three-dimensional space. The approach is demonstrated with the chaperone ERp29, for which large differences have been reported between X-ray and NMR structures of the C-terminal domain, ERp29-C. The results unambiguously show that the structure of rat ERp29-C in solution is similar to the crystal structure of human ERp29-C. PCSs of backbone amides were the only structural restraints required. Because these can be measured for more dilute protein solutions than other NMR restraints, the approach greatly widens the range of proteins amenable to structural studies in solution.

PubMed: 23643949
DOI: 10.1016/j.str.2013.04.001

Experimental method

SOLUTION NMR