Summary for 2MF9
| Entry DOI | 10.2210/pdb2mf9/pdb |
| NMR Information | BMRB: 6923 |
| Descriptor | Peptidyl-prolyl cis-trans isomerase FKBP8 (1 entity in total) |
| Functional Keywords | beta barrel, central helix, flexible n-terminal extension, apoptosis, isomerase |
| Biological source | Homo sapiens (human) |
| Cellular location | Isoform 1: Mitochondrion membrane; Single- pass membrane protein; Cytoplasmic side. Isoform 3: Mitochondrion membrane; Single- pass membrane protein; Cytoplasmic side: Q14318 |
| Total number of polymer chains | 1 |
| Total formula weight | 16910.13 |
| Authors | Kang, C.,Ye, H.,Simon, B.,Sattler, M.,Yoon, H.S. (deposition date: 2013-10-08, release date: 2013-11-06, Last modification date: 2024-05-01) |
| Primary citation | Kang, C.,Ye, H.,Chia, J.,Choi, B.H.,Dhe-Paganon, S.,Simon, B.,Schutz, U.,Sattler, M.,Yoon, H.S. Functional role of the flexible N-terminal extension of FKBP38 in catalysis. Sci Rep, 3:2985-2985, 2013 Cited by PubMed Abstract: FKBP38 regulates apoptosis through unique interactions with multiple regulators including Bcl-2. Interestingly, the peptidylprolyl isomerase activity of FKBP38 is only detectable when it binds to calcium-saturated calmodulin (CaM/Ca(2+)). This, in turn, permits the formation of a complex with Bcl-2. FKBP38 thereby provides an important link between isomerase activity and apoptotic pathways. Here, we show that the N-terminal extension (residues 1-32) preceding the catalytic domain of FKBP38 has an autoinhibitory activity. The core isomerase activity of FKBP38 is inhibited by transient interactions involving the flexible N-terminal extension that precedes the catalytic domain. Notably, CaM/Ca(2+) binds to this N-terminal extension and thereby releases the autoinhibitory contacts between the N-terminal extension and the catalytic domain, thus potentiating the isomerase activity of FKBP38. Our data demonstrate how CaM/Ca(2+) modulates the catalytic activity of FKBP38. PubMed: 24145868DOI: 10.1038/srep02985 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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