2M08
The solution structure of NmPin, the parvuline of Nitrosopumilus maritimus
Summary for 2M08
| Entry DOI | 10.2210/pdb2m08/pdb |
| NMR Information | BMRB: 18801 |
| Descriptor | PpiC-type peptidyl-prolyl cis-trans isomerase (1 entity in total) |
| Functional Keywords | parvulin, archaeal, membrane, thaumarchaeota, sdpar, isomerase |
| Biological source | Nitrosopumilus maritimus |
| Total number of polymer chains | 1 |
| Total formula weight | 10197.92 |
| Authors | Lederer, C.,Bayer, P. (deposition date: 2012-10-22, release date: 2014-04-23, Last modification date: 2024-05-15) |
| Primary citation | Hoppstock, L.,Trusch, F.,Lederer, C.,van West, P.,Koenneke, M.,Bayer, P. NmPin from the marine thaumarchaeote Nitrosopumilus maritimus is an active membrane associated prolyl isomerase. Bmc Biol., 14:53-53, 2016 Cited by PubMed Abstract: Peptidyl-prolyl isomerases (PPIases) are present in all forms of life and play a crucial role in protein folding and regulation. They catalyze the cis-trans isomerization of the peptide bond that precedes proline residues in numerous proteins. The parvulins, which is one family of PPIases, have been extensively investigated in several eukaryotes. However, nothing is known about their expression, function and localization in archaea. PubMed: 27349962DOI: 10.1186/s12915-016-0274-1 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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