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PDBsum entry 2r65
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Contents |
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* Residue conservation analysis
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PDB id:
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Hydrolase
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Title:
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Crystal structure of helicobacter pylori atp dependent protease, ftsh adp complex
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Structure:
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Cell division protease ftsh homolog. Chain: a, b, c, d, e. Fragment: atpase domain, unp residues 160-419. Engineered: yes. Mutation: yes
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Source:
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Helicobacter pylori. Campylobacter pylori. Organism_taxid: 210. Gene: ftsh. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Resolution:
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3.30Å
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R-factor:
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0.290
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R-free:
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0.331
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Authors:
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S.H.Kim,G.B.Kang,H.-E.Song,S.J.Park,M.-H.Bae,S.H.Eom
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Key ref:
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S.H.Kim
et al.
(2008).
Structural studies on Helicobacter pyloriATP-dependent protease, FtsH.
J Synchrotron Radiat,
15,
208-210.
PubMed id:
DOI:
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Date:
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05-Sep-07
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Release date:
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09-Sep-08
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PROCHECK
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Headers
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References
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P71408
(FTSH_HELPY) -
ATP-dependent zinc metalloprotease FtsH from Helicobacter pylori (strain ATCC 700392 / 26695)
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Seq:
Struc:
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632 a.a.
249 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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DOI no:
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J Synchrotron Radiat
15:208-210
(2008)
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PubMed id:
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Structural studies on Helicobacter pyloriATP-dependent protease, FtsH.
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S.H.Kim,
G.B.Kang,
H.E.Song,
S.J.Park,
M.H.Bea,
S.H.Eom.
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ABSTRACT
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The ATP-dependent protease, FtsH, degrades misassembled membrane proteins for
quality control like SecY, subunit a of FoF1-ATPase, and YccA, and digests
short-lived soluble proteins in order to control their cellular regulation,
including sigma32, LpxC and lambdacII. The FtsH protein has an N-terminal
transmembrane segment and a large cytosolic region that consists of two domains,
an ATPase and a protease domain. To provide a structural basis for the
nucleotide-dependent domain motions and a better understanding of substrate
translocation, the crystal structures of the Helicobacter pylori (Hp) FtsH
ATPase domain in the nucleotide-free state and complexed with ADP, were
determined. Two different structures of HpFtsH ATPase were observed, with the
nucleotide-free state in an asymmetric unit, and these structures reveal the new
forms and show other conformational differences between the nucleotide-free and
ADP-bound state compared with previous structures. In particular, one HpFtsH Apo
structure has a considerable rotation difference compared with the HpFtsH ADP
complex, and this large conformational change reveals that FtsH may have the
mechanical force needed for substrate translocation.
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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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A.Karnataki,
A.E.DeRocher,
J.E.Feagin,
and
M.Parsons
(2009).
Sequential processing of the Toxoplasma apicoplast membrane protein FtsH1 in topologically distinct domains during intracellular trafficking.
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Mol Biochem Parasitol,
166,
126-133.
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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.
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Links
