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PDBsum entry 2fbn
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Structural genomics, unknown function
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PDB id
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2fbn
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Contents |
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* Residue conservation analysis
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PDB id:
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Structural genomics, unknown function
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Title:
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Plasmodium falciparum putative fk506-binding protein pfl2275c, c- terminal tpr-containing domain
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Structure:
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70 kda peptidylprolyl isomerase, putative. Chain: a, b. Engineered: yes
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Source:
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Plasmodium falciparum. Malaria parasite p. Falciparum. Organism_taxid: 5833. Expressed in: escherichia coli. Expression_system_taxid: 511693. Pet28
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Biol. unit:
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Dimer (from
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Resolution:
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1.63Å
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R-factor:
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0.201
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R-free:
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0.235
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Authors:
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A.Dong,J.Lew,I.Koeieradzki,E.Sundararajan,M.Melone,G.Wasney,Y.Zhao, A.M.Edwards,C.H.Arrowsmith,J.Weigelt,M.Sundstrom,A.Bochkarev,R.Hui, T.Hills,Structural Genomics Consortium (Sgc)
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Key ref:
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R.Alag
et al.
(2009).
Crystallographic structure of the tetratricopeptide repeat domain of Plasmodium falciparum FKBP35 and its molecular interaction with Hsp90 C-terminal pentapeptide.
Protein Sci,
18,
2115-2124.
PubMed id:
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Date:
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09-Dec-05
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Release date:
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24-Jan-06
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PROCHECK
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Headers
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References
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Q8I4V8
(Q8I4V8_PLAF7) -
Peptidyl-prolyl cis-trans isomerase FKBP35 from Plasmodium falciparum (isolate 3D7)
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Seq:
Struc:
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304 a.a.
153 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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Protein Sci
18:2115-2124
(2009)
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PubMed id:
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Crystallographic structure of the tetratricopeptide repeat domain of Plasmodium falciparum FKBP35 and its molecular interaction with Hsp90 C-terminal pentapeptide.
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R.Alag,
N.Bharatham,
A.Dong,
T.Hills,
A.Harikishore,
A.A.Widjaja,
S.G.Shochat,
R.Hui,
H.S.Yoon.
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ABSTRACT
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Plasmodium falciparum FK506-binding protein 35 (PfFKBP35) that binds to FK506
contains a conserved tetratricopeptide repeat (TPR) domain. Several known TPR
domains such as Hop, PPP5, CHIP, and FKBP52 are structurally conserved and are
able to interact with molecular chaperones such as Hsp70/Hsp90. Here, we present
the crystal structure of PfFKBP35-TPR and demonstrate its interaction with Hsp90
C-terminal pentapeptide (MEEVD) by surface plasmon resonance and nuclear
magnetic resonance spectroscopy-based binding studies. Our sequence and
structural analyses reveal that PfFKBP35 is similar to Hop and PPP5 in
possessing all the conserved residues which are important for carboxylate
clamping with Hsp90. Mutational studies were carried out on positively charged
clamp residues that are crucial for binding to carboxylate groups of aspartate,
showing that all the mutated residues are important for Hsp90 binding. Molecular
docking and electrostatic calculations demonstrated that the MEEVD peptide of
Hsp90 can form aspartate clamp unlike FKBP52. Our results provide insightful
information and structural basis about the molecular interaction between
PfFKBP35-TPR and Hsp90.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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R.Alag,
I.A.Qureshi,
N.Bharatham,
J.Shin,
J.Lescar,
and
H.S.Yoon
(2010).
NMR and crystallographic structures of the FK506 binding domain of human malarial parasite Plasmodium vivax FKBP35.
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Protein Sci,
19,
1577-1586.
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PDB code:
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X.Yang,
T.R.Lenhart,
T.Kariu,
J.Anguita,
D.R.Akins,
and
U.Pal
(2010).
Characterization of unique regions of Borrelia burgdorferi surface-located membrane protein 1.
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Infect Immun,
78,
4477-4487.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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Links
