PDBsum entry 2mf9

Apoptosis, isomerase

PDB id: 2mf9

Contents

Protein chain

157 a.a.

PDB id:

2mf9

Name:

Apoptosis, isomerase

Title:

Solution structure of the n-terminal domain of human fkbp38 (fkbp38ntd)

Structure:

Peptidyl-prolyl cis-trans isomerase fkbp8. Chain: a. Fragment: unp residues 58-206. Synonym: ppiase fkbp8, 38 kda fk506-binding protein, 38 kda fkbp, fkbp-38, hfkbp38, fk506-binding protein 8, fkbp-8, fkbpr38, rotamase. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: fkbp8, fkbp38. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

C.Kang,H.Ye,B.Simon,M.Sattler,H.S.Yoon

Key ref:

C.Kang et al. (2013). Functional role of the flexible N-terminal extension of FKBP38 in catalysis. Sci Rep, 3, 2985. PubMed id: 24145868 DOI: 10.1038/srep02985

Date:

08-Oct-13 Release date: 06-Nov-13

Supersedes:

2jwx

Protein chain

Q14318  (FKBP8_HUMAN) -  Peptidyl-prolyl cis-trans isomerase FKBP8 from Homo sapiens

Seq: 412 a.a.

Struc: 157 a.a.*

* PDB and UniProt seqs differ at 9 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.5.2.1.8 - peptidylprolyl isomerase.
• Reaction: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

DOI no: 10.1038/srep02985

Sci Rep 3:2985 (2013)

PubMed id: 24145868

Functional role of the flexible N-terminal extension of FKBP38 in catalysis.

C.Kang, H.Ye, J.Chia, B.H.Choi, S.Dhe-Paganon, B.Simon, U.Schütz, M.Sattler, H.S.Yoon.

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.