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PDBsum entry 1r7r
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Transport protein
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PDB id
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1r7r
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Contents |
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* Residue conservation analysis
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PDB id:
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Transport protein
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Title:
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The crystal structure of murine p97/vcp at 3.6a
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Structure:
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Transitional endoplasmic reticulum atpase. Chain: a. Synonym: ter atpase, 15s mg(2+)-atpase p97 subunit, valosin containing protein, vcp. Engineered: yes
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Source:
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Mus musculus. House mouse. Organism_taxid: 10090. Gene: vcp. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Biol. unit:
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Hexamer (from PDB file)
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Resolution:
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3.60Å
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R-factor:
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0.327
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R-free:
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0.358
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Authors:
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T.Huyton,V.E.Pye,L.C.Briggs,T.C.Flynn,F.Beuron,H.Kondo,J.Ma,X.Zhang, P.S.Freemont
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Key ref:
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T.Huyton
et al.
(2003).
The crystal structure of murine p97/VCP at 3.6A.
J Struct Biol,
144,
337-348.
PubMed id:
DOI:
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Date:
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22-Oct-03
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Release date:
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16-Dec-03
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PROCHECK
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Headers
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References
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Q01853
(TERA_MOUSE) -
Transitional endoplasmic reticulum ATPase from Mus musculus
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Seq: Struc:
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806 a.a.
683 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 6 residue positions (black
crosses)
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Enzyme class:
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E.C.3.6.4.6
- vesicle-fusing ATPase.
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Reaction:
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ATP + H2O = ADP + phosphate + H+
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ATP
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+
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H2O
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=
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ADP
Bound ligand (Het Group name = )
corresponds exactly
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+
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phosphate
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+
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H(+)
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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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J Struct Biol
144:337-348
(2003)
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PubMed id:
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The crystal structure of murine p97/VCP at 3.6A.
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T.Huyton,
V.E.Pye,
L.C.Briggs,
T.C.Flynn,
F.Beuron,
H.Kondo,
J.Ma,
X.Zhang,
P.S.Freemont.
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ABSTRACT
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p97/VCP is a member of the AAA ATPase family and has roles in both membrane
fusion and ubiquitin dependent protein degradation. Here, we present a 3.6A
crystal structure of murine p97 in which D2 domain has been modelled as
poly-alanine and the remaining approximately 100 residues are absent. The
resulting structure illustrates a head-to-tail packing arrangement of the two
p97 AAA domains in a natural hexameric state with D1 ADP bound and D2 nucleotide
free. The head-to-tail packing arrangement observed in this structure is in
contrast to our previously predicted tail-to-tail packing model. The linker
between the D1 and D2 domains is partially disordered, suggesting a flexible
nature. Normal mode analysis of the crystal structure suggests anti-correlated
motions and distinct conformational states of the two AAA domains.
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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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L.F.Chang,
S.Chen,
C.C.Liu,
X.Pan,
J.Jiang,
X.C.Bai,
X.Xie,
H.W.Wang,
and
S.F.Sui
(2012).
Structural characterization of full-length NSF and 20S particles.
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Nat Struct Mol Biol,
19,
268-275.
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T.F.Chou,
S.J.Brown,
D.Minond,
B.E.Nordin,
K.Li,
A.C.Jones,
P.Chase,
P.R.Porubsky,
B.M.Stoltz,
F.J.Schoenen,
M.P.Patricelli,
P.Hodder,
H.Rosen,
and
R.J.Deshaies
(2011).
Reversible inhibitor of p97, DBeQ, impairs both ubiquitin-dependent and autophagic protein clearance pathways.
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Proc Natl Acad Sci U S A,
108,
4834-4839.
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C.A.Ewens,
P.Kloppsteck,
A.Förster,
X.Zhang,
and
P.S.Freemont
(2010).
Structural and functional implications of phosphorylation and acetylation in the regulation of the AAA+ protein p97.
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Biochem Cell Biol,
88,
41-48.
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D.S.Haines
(2010).
p97-containing complexes in proliferation control and cancer: emerging culprits or guilt by association?
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Genes Cancer,
1,
753-763.
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I.Stokes-Rees,
and
P.Sliz
(2010).
Protein structure determination by exhaustive search of Protein Data Bank derived databases.
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Proc Natl Acad Sci U S A,
107,
21476-21481.
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P.Wendler,
and
H.R.Saibil
(2010).
Cryo electron microscopy structures of Hsp100 proteins: crowbars in or out?
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Biochem Cell Biol,
88,
89-96.
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T.Haslberger,
B.Bukau,
and
A.Mogk
(2010).
Towards a unifying mechanism for ClpB/Hsp104-mediated protein disaggregation and prion propagation.
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Biochem Cell Biol,
88,
63-75.
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W.K.Tang,
D.Li,
C.C.Li,
L.Esser,
R.Dai,
L.Guo,
and
D.Xia
(2010).
A novel ATP-dependent conformation in p97 N-D1 fragment revealed by crystal structures of disease-related mutants.
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EMBO J,
29,
2217-2229.
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PDB codes:
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A.T.Brunger,
B.Delabarre,
J.M.Davies,
and
W.I.Weis
(2009).
X-ray structure determination at low resolution.
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Acta Crystallogr D Biol Crystallogr,
65,
128-133.
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G.Effantin,
R.Rosenzweig,
M.H.Glickman,
and
A.C.Steven
(2009).
Electron microscopic evidence in support of alpha-solenoid models of proteasomal subunits Rpn1 and Rpn2.
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J Mol Biol,
386,
1204-1211.
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M.J.Landsberg,
P.R.Vajjhala,
R.Rothnagel,
A.L.Munn,
and
B.Hankamer
(2009).
Three-dimensional structure of AAA ATPase Vps4: advancing structural insights into the mechanisms of endosomal sorting and enveloped virus budding.
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Structure,
17,
427-437.
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R.Ernst,
B.Mueller,
H.L.Ploegh,
and
C.Schlieker
(2009).
The otubain YOD1 is a deubiquitinating enzyme that associates with p97 to facilitate protein dislocation from the ER.
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Mol Cell,
36,
28-38.
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W.K.Tang,
D.Li,
L.Esser,
and
D.Xia
(2009).
Purification, crystallization and preliminary X-ray diffraction analysis of disease-related mutants of p97.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
65,
1166-1170.
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C.Cho,
S.L.Reck-Peterson,
and
R.D.Vale
(2008).
Regulatory ATPase sites of cytoplasmic dynein affect processivity and force generation.
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J Biol Chem,
283,
25839-25845.
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J.M.Davies,
A.T.Brunger,
and
W.I.Weis
(2008).
Improved structures of full-length p97, an AAA ATPase: implications for mechanisms of nucleotide-dependent conformational change.
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Structure,
16,
715-726.
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PDB codes:
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L.C.Briggs,
G.S.Baldwin,
N.Miyata,
H.Kondo,
X.Zhang,
and
P.S.Freemont
(2008).
Analysis of nucleotide binding to P97 reveals the properties of a tandem AAA hexameric ATPase.
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J Biol Chem,
283,
13745-13752.
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M.D.Gonciarz,
F.G.Whitby,
D.M.Eckert,
C.Kieffer,
A.Heroux,
W.I.Sundquist,
and
C.P.Hill
(2008).
Biochemical and structural studies of yeast Vps4 oligomerization.
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J Mol Biol,
384,
878-895.
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PDB codes:
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Z.Yu,
M.D.Gonciarz,
W.I.Sundquist,
C.P.Hill,
and
G.J.Jensen
(2008).
Cryo-EM structure of dodecameric Vps4p and its 2:1 complex with Vta1p.
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J Mol Biol,
377,
364-377.
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C.Zhao,
J.T.Slevin,
and
S.W.Whiteheart
(2007).
Cellular functions of NSF: not just SNAPs and SNAREs.
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FEBS Lett,
581,
2140-2149.
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M.Kavoosi,
A.L.Creagh,
D.G.Kilburn,
and
C.A.Haynes
(2007).
Strategy for selecting and characterizing linker peptides for CBM9-tagged fusion proteins expressed in Escherichia coli.
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Biotechnol Bioeng,
98,
599-610.
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P.Wendler,
J.Shorter,
C.Plisson,
A.G.Cashikar,
S.Lindquist,
and
H.R.Saibil
(2007).
Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104.
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Cell,
131,
1366-1377.
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R.L.Isaacson,
V.E.Pye,
P.Simpson,
H.H.Meyer,
X.Zhang,
P.S.Freemont,
and
S.Matthews
(2007).
Detailed structural insights into the p97-Npl4-Ufd1 interface.
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J Biol Chem,
282,
21361-21369.
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PDB code:
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S.Lee,
J.M.Choi,
and
F.T.Tsai
(2007).
Visualizing the ATPase cycle in a protein disaggregating machine: structural basis for substrate binding by ClpB.
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Mol Cell,
25,
261-271.
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V.E.Pye,
F.Beuron,
C.A.Keetch,
C.McKeown,
C.V.Robinson,
H.H.Meyer,
X.Zhang,
and
P.S.Freemont
(2007).
Structural insights into the p97-Ufd1-Npl4 complex.
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Proc Natl Acad Sci U S A,
104,
467-472.
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B.DeLaBarre,
and
A.T.Brunger
(2006).
Considerations for the refinement of low-resolution crystal structures.
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Acta Crystallogr D Biol Crystallogr,
62,
923-932.
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B.DeLaBarre,
J.C.Christianson,
R.R.Kopito,
and
A.T.Brunger
(2006).
Central pore residues mediate the p97/VCP activity required for ERAD.
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Mol Cell,
22,
451-462.
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C.Hicks-Berger,
I.Sokolchik,
C.Kim,
and
D.J.Morré
(2006).
A plasma membrane-associated AAA-ATPase from Glycine max.
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Biofactors,
28,
135-149.
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D.J.Morré,
C.Kim,
and
C.Hicks-Berger
(2006).
ATP-dependent and drug-inhibited vesicle enlargement reconstituted using synthetic lipids and recombinant proteins.
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Biofactors,
28,
105-117.
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F.Beuron,
I.Dreveny,
X.Yuan,
V.E.Pye,
C.McKeown,
L.C.Briggs,
M.J.Cliff,
Y.Kaneko,
R.Wallis,
R.L.Isaacson,
J.E.Ladbury,
S.J.Matthews,
H.Kondo,
X.Zhang,
and
P.S.Freemont
(2006).
Conformational changes in the AAA ATPase p97-p47 adaptor complex.
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EMBO J,
25,
1967-1976.
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G.Li,
G.Zhao,
X.Zhou,
H.Schindelin,
and
W.J.Lennarz
(2006).
The AAA ATPase p97 links peptide N-glycanase to the endoplasmic reticulum-associated E3 ligase autocrine motility factor receptor.
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Proc Natl Acad Sci U S A,
103,
8348-8353.
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J.P.Erzberger,
and
J.M.Berger
(2006).
Evolutionary relationships and structural mechanisms of AAA+ proteins.
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Annu Rev Biophys Biomol Struct,
35,
93.
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M.Rappas,
J.Schumacher,
H.Niwa,
M.Buck,
and
X.Zhang
(2006).
Structural basis of the nucleotide driven conformational changes in the AAA+ domain of transcription activator PspF.
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J Mol Biol,
357,
481-492.
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PDB codes:
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A.Gerega,
B.Rockel,
J.Peters,
T.Tamura,
W.Baumeister,
and
P.Zwickl
(2005).
VAT, the thermoplasma homolog of mammalian p97/VCP, is an N domain-regulated protein unfoldase.
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J Biol Chem,
280,
42856-42862.
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B.Nagar,
and
J.Kuriyan
(2005).
SAXS and the working protein.
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Structure,
13,
169-170.
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H.Richly,
M.Rape,
S.Braun,
S.Rumpf,
C.Hoege,
and
S.Jentsch
(2005).
A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting.
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Cell,
120,
73-84.
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J.M.Davies,
H.Tsuruta,
A.P.May,
and
W.I.Weis
(2005).
Conformational changes of p97 during nucleotide hydrolysis determined by small-angle X-Ray scattering.
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Structure,
13,
183-195.
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S.Elsasser,
and
D.Finley
(2005).
Delivery of ubiquitinated substrates to protein-unfolding machines.
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Nat Cell Biol,
7,
742-749.
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D.M.Rancour,
S.Park,
S.D.Knight,
and
S.Y.Bednarek
(2004).
Plant UBX domain-containing protein 1, PUX1, regulates the oligomeric structure and activity of arabidopsis CDC48.
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J Biol Chem,
279,
54264-54274.
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I.Dreveny,
H.Kondo,
K.Uchiyama,
A.Shaw,
X.Zhang,
and
P.S.Freemont
(2004).
Structural basis of the interaction between the AAA ATPase p97/VCP and its adaptor protein p47.
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EMBO J,
23,
1030-1039.
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PDB code:
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K.Shiozawa,
N.Maita,
K.Tomii,
A.Seto,
N.Goda,
Y.Akiyama,
T.Shimizu,
M.Shirakawa,
and
H.Hiroaki
(2004).
Structure of the N-terminal domain of PEX1 AAA-ATPase. Characterization of a putative adaptor-binding domain.
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J Biol Chem,
279,
50060-50068.
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PDB code:
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R.M.Bruderer,
C.Brasseur,
and
H.H.Meyer
(2004).
The AAA ATPase p97/VCP interacts with its alternative co-factors, Ufd1-Npl4 and p47, through a common bipartite binding mechanism.
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J Biol Chem,
279,
49609-49616.
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S.L.Kazmirski,
M.Podobnik,
T.F.Weitze,
M.O'Donnell,
and
J.Kuriyan
(2004).
Structural analysis of the inactive state of the Escherichia coli DNA polymerase clamp-loader complex.
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Proc Natl Acad Sci U S A,
101,
16750-16755.
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PDB codes:
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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
codes are
shown on the right.
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}
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