 |
PDBsum entry 3a57
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
|
PDB id:
|
|
|
|
| Name: |
|
Toxin
|
|
|
Title:
|
|
Crystal structure of thermostable direct hemolysin
|
|
Structure:
|
|
Thermostable direct hemolysin 2. Chain: a. Synonym: thermostable direct hemolysin, kanagawa phenomenon- associated hemolysin. Engineered: yes
|
|
Source:
|
|
Vibrio parahaemolyticus. Organism_taxid: 670. Gene: tdh. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
Resolution:
|
|
|
1.50Å
|
R-factor:
|
0.134
|
R-free:
|
0.170
|
|
|
Authors:
|
|
H.Hashimoto,I.Yanagihara,K.Nakahira,D.Hamada,T.Ikegami,K.Mayanagi, S.Kaieda,T.Fukui,K.Ohnishi,S.Kajiyama,T.Yamane,M.Ikeguchi,T.Honda, T.Shimizu,M.Sato
|
|
Key ref:
|
|
I.Yanagihara
et al.
(2010).
Structure and functional characterization of Vibrio parahaemolyticus thermostable direct hemolysin.
J Biol Chem,
285,
16267-16274.
PubMed id:
|
|
|
Date:
|
|
|
03-Aug-09
|
Release date:
|
31-Mar-10
|
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
|
Headers
|
|
|
|
References
|
|
|
|
|
|
|
|
P19250
(HLY2_VIBPA) -
Thermostable direct hemolysin 2 from Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
|
|
|
|
Seq:
Struc:
|
|
|
|
189 a.a.
154 a.a.*
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Key: |
 |
PfamA domain |
|
|
 |
Secondary structure |
|
 |
CATH domain |
|
|
*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
|
J Biol Chem
285:16267-16274
(2010)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Structure and functional characterization of Vibrio parahaemolyticus thermostable direct hemolysin.
|
|
I.Yanagihara,
K.Nakahira,
T.Yamane,
S.Kaieda,
K.Mayanagi,
D.Hamada,
T.Fukui,
K.Ohnishi,
S.Kajiyama,
T.Shimizu,
M.Sato,
T.Ikegami,
M.Ikeguchi,
T.Honda,
H.Hashimoto.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
Thermostable direct hemolysin (TDH) is a major virulence factor of Vibrio
parahaemolyticus that causes pandemic foodborne enterocolitis mediated by
seafood. TDH exists as a tetramer in solution, and it possesses extreme
hemolytic activity. Here, we present the crystal structure of the TDH tetramer
at 1.5 A resolution. The TDH tetramer forms a central pore with dimensions of 23
A in diameter and approximately 50 A in depth. Pi-cation interactions between
protomers comprising the tetramer were indispensable for hemolytic activity of
TDH. The N-terminal region was intrinsically disordered outside of the pore.
Molecular dynamic simulations suggested that water molecules permeate freely
through the central and side channel pores. Electron micrographs showed that
tetrameric TDH attached to liposomes, and some of the tetramer associated with
liposome via one protomer. These findings imply a novel membrane attachment
mechanism by a soluble tetrameric pore-forming toxin.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Literature references that cite this PDB file's key reference
|
|
|
| |
PubMed id
|
|
Reference
|
|
|
|
|
|
K.Ohnishi,
K.Nakahira,
S.Unzai,
K.Mayanagi,
H.Hashimoto,
K.Shiraki,
T.Honda,
and
I.Yanagihara
(2011).
Relationship between heat-induced fibrillogenicity and hemolytic activity of thermostable direct hemolysin and a related hemolysin of Vibrio parahaemolyticus.
|
| |
FEMS Microbiol Lett,
318,
10-17.
|
|
|
|
|
|
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.
|
|
Links
