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PDBsum entry 4msp
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PDB id:
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Isomerase
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Title:
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Crystal structure of human peptidyl-prolyl cis-trans isomerase fkbp22 (aka fkbp14) containing two ef-hand motifs
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Structure:
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Peptidyl-prolyl cis-trans isomerase fkbp14. Chain: a, b. Synonym: ppiase fkbp14, 22 kda fk506-binding protein, 22 kda fkbp, fkbp-22, fk506-binding protein 14, fkbp-14, rotamase. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: fkbp14, fkbp22, unq322/pro381. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Resolution:
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1.90Å
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R-factor:
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0.160
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R-free:
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0.200
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Authors:
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S.P.Boudko,Y.Ishikawa,H.P.Bachinger
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Key ref:
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S.P.Boudko
et al.
(2014).
Structure of human peptidyl-prolyl cis-trans isomerase FKBP22 containing two EF-hand motifs.
Protein Sci,
23,
67-75.
PubMed id:
DOI:
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Date:
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18-Sep-13
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Release date:
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25-Dec-13
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PROCHECK
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Headers
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References
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Q9NWM8
(FKB14_HUMAN) -
Peptidyl-prolyl cis-trans isomerase FKBP14 from Homo sapiens
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Seq:
Struc:
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211 a.a.
189 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Enzyme class:
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E.C.5.2.1.8
- peptidylprolyl isomerase.
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Reaction:
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[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
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Peptidylproline (omega=180)
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=
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peptidylproline (omega=0)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Protein Sci
23:67-75
(2014)
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PubMed id:
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Structure of human peptidyl-prolyl cis-trans isomerase FKBP22 containing two EF-hand motifs.
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S.P.Boudko,
Y.Ishikawa,
J.Nix,
M.S.Chapman,
H.P.Bächinger.
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ABSTRACT
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The FK506-binding protein (FKBP) family consists of proteins with a variety of
protein-protein interaction domains and versatile cellular functions. It is
assumed that all members are peptidyl-prolyl cis-trans isomerases with the
enzymatic function attributed to the FKBP domain. Six members of this family
localize to the mammalian endoplasmic reticulum (ER). Four of them, FKBP22
(encoded by the FKBP14 gene), FKBP23 (FKBP7), FKBP60 (FKBP9), and FKBP65
(FKBP10), are unique among all FKBPs as they contain the EF-hand motifs. Little
is known about the biological roles of these proteins, but emerging genetics
studies are attracting great interest to the ER resident FKBPs, as mutations in
genes encoding FKBP10 and FKBP14 were shown to cause a variety of matrix
disorders. Although the structural organization of the FKBP-type domain as well
as of the EF-hand motif has been known for a while, it is difficult to conclude
how these structures are combined and how it affects the protein functionality.
We have determined a unique 1.9 Å resolution crystal structure for human
FKBP22, which can serve as a prototype for other EF hand-containing FKBPs. The
EF-hand motifs of two FKBP22 molecules form a dimeric complex with an elongated
and predominantly hydrophobic cavity that can potentially be occupied by an
aliphatic ligand. The FKBP-type domains are separated by a cleft and their
putative active sites can catalyze isomerazation of two bonds within a
polypeptide chain in extended conformation. These structural results are of
prime interest for understanding biological functions of ER resident FKBPs
containing EF-hand motifs.
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