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2M08

The solution structure of NmPin, the parvuline of Nitrosopumilus maritimus

Summary for 2M08
Entry DOI10.2210/pdb2m08/pdb
NMR InformationBMRB: 18801
DescriptorPpiC-type peptidyl-prolyl cis-trans isomerase (1 entity in total)
Functional Keywordsparvulin, archaeal, membrane, thaumarchaeota, sdpar, isomerase
Biological sourceNitrosopumilus maritimus
Total number of polymer chains1
Total formula weight10197.92
Authors
Lederer, C.,Bayer, P. (deposition date: 2012-10-22, release date: 2014-04-23, Last modification date: 2024-05-15)
Primary citationHoppstock, 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: 27349962
DOI: 10.1186/s12915-016-0274-1
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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