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PDBsum entry 4o8i
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PDB id:
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Isomerase
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Title:
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1.45a resolution structure of peg 400 bound cyclophilin d
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Structure:
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Peptidyl-prolyl cis-trans isomerase f, mitochondrial. Chain: a. Synonym: ppiase f, cyclophilin d, cyp-d, cypd, cyclophilin f, mitochondrial cyclophilin, cyp-m, rotamase f. Engineered: yes. Mutation: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: ppif, cyp3. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Resolution:
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1.45Å
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R-factor:
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0.161
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R-free:
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0.190
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Authors:
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S.Lovell,K.R.Valasani,K.P.Battaile,C.Wang,S.S.Yan
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Key ref:
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K.R.Valasani
et al.
(2014).
High-resolution crystal structures of two crystal forms of human cyclophilin D in complex with PEG 400 molecules.
Acta Crystallogr F Struct Biol Commun,
70,
717-722.
PubMed id:
DOI:
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Date:
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27-Dec-13
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Release date:
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11-Jun-14
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PROCHECK
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Headers
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References
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P30405
(PPIF_HUMAN) -
Peptidyl-prolyl cis-trans isomerase F, mitochondrial from Homo sapiens
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Seq:
Struc:
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207 a.a.
164 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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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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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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Acta Crystallogr F Struct Biol Commun
70:717-722
(2014)
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PubMed id:
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High-resolution crystal structures of two crystal forms of human cyclophilin D in complex with PEG 400 molecules.
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K.R.Valasani,
E.A.Carlson,
K.P.Battaile,
A.Bisson,
C.Wang,
S.Lovell,
S.ShiDu Yan.
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ABSTRACT
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Cyclophilin D (CypD) is a key mitochondrial target for amyloid-β-induced
mitochondrial and synaptic dysfunction and is considered a potential drug target
for Alzheimer's disease. The high-resolution crystal structures of primitive
orthorhombic (CypD-o) and primitive tetragonal (CypD-t) forms have been
determined to 1.45 and 0.85 Å resolution, respectively, and are nearly
identical structurally. Although an isomorphous structure of CypD-t has
previously been reported, the structure reported here was determined at atomic
resolution, while CypD-o represents a new crystal form for this protein. In
addition, each crystal form contains a PEG 400 molecule bound to the same region
along with a second PEG 400 site in CypD-t which occupies the cyclosporine A
inhibitor binding site of CypD. Highly precise structural information for CypD
should be extremely useful for discerning the detailed interaction of small
molecules, particularly drugs and/or inhibitors, bound to CypD. The 0.85 Å
resolution structure of CypD-t is the highest to date for any CypD structure.
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