3UI5
Crystal structure of human Parvulin 14
Summary for 3UI5
| Entry DOI | 10.2210/pdb3ui5/pdb |
| Related | 3UI4 3UI6 |
| Descriptor | Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4, SULFATE ION, (4S,5S)-1,2-DITHIANE-4,5-DIOL, ... (5 entities in total) |
| Functional Keywords | peptidyl-prolyl-isomerase, isomerase |
| Biological source | Homo sapiens (human) |
| Cellular location | Isoform 1: Nucleus, nucleolus. Isoform 2: Mitochondrion: Q9Y237 |
| Total number of polymer chains | 1 |
| Total formula weight | 11743.51 |
| Authors | Mueller, J.W.,Link, N.M.,Matena, A.,Hoppstock, L.,Rueppel, A.,Bayer, P.,Blankenfeldt, W. (deposition date: 2011-11-04, release date: 2011-12-07, Last modification date: 2024-02-28) |
| Primary citation | Mueller, J.W.,Link, N.M.,Matena, A.,Hoppstock, L.,Ruppel, A.,Bayer, P.,Blankenfeldt, W. Crystallographic proof for an extended hydrogen-bonding network in small prolyl isomerases. J.Am.Chem.Soc., 133:20096-20099, 2011 Cited by PubMed Abstract: Parvulins compose a family of small peptidyl-prolyl isomerases (PPIases) involved in protein folding and protein quality control. A number of amino acids in the catalytic cavity are highly conserved, but their precise role within the catalytic mechanism is unknown. The 0.8 Å crystal structure of the prolyl isomerase domain of parvulin Par14 shows the electron density of hydrogen atoms between the D74, H42, H123, and T118 side chains. This threonine residue has previously not been associated with catalysis, but a corresponding T152A mutant of Pin1 shows a dramatic reduction of catalytic activity without compromising protein stability. The observed catalytic tetrad is strikingly conserved in Pin1- and parvulin-type proteins and hence constitutes a common feature of small peptidyl prolyl isomerases. PubMed: 22081960DOI: 10.1021/ja2086195 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
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