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Atp-binding protein
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PDB id
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2fna
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Contents |
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* Residue conservation analysis
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Gene Ontology (GO) functional annotation
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Biochemical function
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nucleotide binding
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2 terms
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DOI no:
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Proteins
74:1041-1049
(2009)
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PubMed id:
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Crystal structure of a novel archaeal AAA+ ATPase SSO1545 from Sulfolobus solfataricus.
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Q.Xu,
C.L.Rife,
D.Carlton,
M.D.Miller,
S.S.Krishna,
M.A.Elsliger,
P.Abdubek,
T.Astakhova,
H.J.Chiu,
T.Clayton,
L.Duan,
J.Feuerhelm,
S.K.Grzechnik,
J.Hale,
G.W.Han,
L.Jaroszewski,
K.K.Jin,
H.E.Klock,
M.W.Knuth,
A.Kumar,
D.McMullan,
A.T.Morse,
E.Nigoghossian,
L.Okach,
S.Oommachen,
J.Paulsen,
R.Reyes,
H.van den Bedem,
K.O.Hodgson,
J.Wooley,
A.M.Deacon,
A.Godzik,
S.A.Lesley,
I.A.Wilson.
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ABSTRACT
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Selected figure(s)
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Figure 2.
Figure 2. Surface conservation pattern and the nucleotide
binding site of SSO1545. A: Molecular surface of SSO1545 colored
by sequence conservation. The most conserved residues are shown
in red, the nonconserved residues in white. The three domains of
SSO1543 are shown in ribbon representation and colored as
yellow, blue, and cyan, respectively. The orientation of left
panel is the same as in Figure 1(A). B: Close-up stereo view of
the ADP binding site. The bound ADP (yellow) and magnesium ion
(silver) are shown in sticks and sphere, respectively. Walker A
(P-loop, green), Walker B (W-B, blue), sensor I (S-I, cyan),
sensor II (S-II, white) are shown in cartoon and sticks. The
STAND-specific hhGRExE and GxP motifs are also highlighted in
blue.
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Figure 3.
Figure 3. Structural comparisons of SSO1545 with AAA+ ATPases
with similar domain organizations: Orc1 (PDB 2v1u), RuvB (PDB
1in5), Orc2 (PDB 1w5t), and Apaf-1 (PDB 1z6t, residues 105-450).
These structures were superimposed base on their respective
NTPase domains (gray). The linker regions connecting the NTPase
domain and the WH domain (green) are shown in red. The
nucleotides and magnesium ions are shown in sticks and spheres,
respectively.
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The above figures are
reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2009,
74,
1041-1049)
copyright 2009.
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Figures were
selected
by an automated process.
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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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E.Marquenet,
and
E.Richet
(2010).
Conserved motifs involved in ATP hydrolysis by MalT, a signal transduction ATPase with numerous domains from Escherichia coli.
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J Bacteriol, 192,
5181-5191.
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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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