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PDBsum entry 1ef4
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* Residue conservation analysis
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Enzyme class:
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E.C.2.7.7.6
- DNA-directed Rna polymerase.
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Reaction:
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RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate
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RNA(n)
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+
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ribonucleoside 5'-triphosphate
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=
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RNA(n+1)
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+
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diphosphate
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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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Proc Natl Acad Sci U S A
97:6316-6321
(2000)
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PubMed id:
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Zinc-bundle structure of the essential RNA polymerase subunit RPB10 from Methanobacterium thermoautotrophicum.
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C.D.Mackereth,
C.H.Arrowsmith,
A.M.Edwards,
L.P.McIntosh.
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ABSTRACT
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The RNA polymerase subunit RPB10 displays a high level of conservation across
archaea and eukarya and is required for cell viability in yeast. Structure
determination of this RNA polymerase subunit from Methanobacterium
thermoautotrophicum reveals a topology, which we term a zinc-bundle, consisting
of three alpha-helices stabilized by a zinc ion. The metal ion is bound within
an atypical CX(2)CX(n)CC sequence motif and serves to bridge an N-terminal loop
with helix 3. This represents an example of two adjacent zinc-binding Cys
residues within an alpha-helix conformation. Conserved surface features of RPB10
include discrete regions of neutral, acidic, and basic residues, the latter
being located around the zinc-binding site. One or more of these regions may
contribute to the role of this subunit as a scaffold protein within the
polymerase holoenzyme.
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Selected figure(s)
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Figure 2.
Fig. 2. NMR-derived zinc-bundle structure of mtRPB10. (A)
The -trace of
20 structures of mtRBP10, superimposed by using the main chain
helical atoms (14-26, 30-37, and 42-48). The helices are
highlighted in red, and the zinc ion is shown as a pink ball.
Every tenth residue is numbered. The N- and C-terminal residues
Met1, Ile2, Glu53, Thr54, and Trp55 are conformationally
flexible in solution, as evident by heteronuclear 1H{15N} NOE
values less than 0.5. (B) Zinc binding site in mtRPB10. (C)
Stereo view of a representative mtRPB10 structure displaying
residues within the hydrophobic core: Leu7 and Val13 in the
N-terminal region, Phe17, Tyr20, and Val24 of helix 1, Pro30,
Val33, Leu34, and Leu37 of helix 2, Leu39 in the loop between
helix 2 and 3, Leu48, Ile49 of helix 3, and Val52 in the
C-terminal region. These conserved residues are shown according
to the color scheme of Fig. 1.
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Figure 4.
Fig. 4. Structural similarity to protein and nucleic acid
binding domains. mtRPB10 is shown with helices 1, 2, and 3
colored red, green, and blue, respectively. The zinc atom is
shown as a pink ball. This color scheme is used to identify
similar helices in the following structurally related proteins
found in the Protein Data Bank: the protein-binding N-terminal
domain of HIV-2 integrase (PDB ID code 1AUB), with the
zinc-chelating Cys and His residues drawn in light gray, and the
zinc atom shown as a pink ball; the DNA-binding homeodomain of
engrailed (PDB ID code 1ENH); and the RNA-binding domain of
ribosome subunit L11 (PDB ID code 1QA6).
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Figures were
selected
by the author.
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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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P.Cramer,
K.J.Armache,
S.Baumli,
S.Benkert,
F.Brueckner,
C.Buchen,
G.E.Damsma,
S.Dengl,
S.R.Geiger,
A.J.Jasiak,
A.Jawhari,
S.Jennebach,
T.Kamenski,
H.Kettenberger,
C.D.Kuhn,
E.Lehmann,
K.Leike,
J.F.Sydow,
and
A.Vannini
(2008).
Structure of eukaryotic RNA polymerases.
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Annu Rev Biophys,
37,
337-352.
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L.Aravind,
V.Anantharaman,
S.Balaji,
M.M.Babu,
and
L.M.Iyer
(2005).
The many faces of the helix-turn-helix domain: transcription regulation and beyond.
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FEMS Microbiol Rev,
29,
231-262.
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E.L.Hendrickson,
R.Kaul,
Y.Zhou,
D.Bovee,
P.Chapman,
J.Chung,
E.Conway de Macario,
J.A.Dodsworth,
W.Gillett,
D.E.Graham,
M.Hackett,
A.K.Haydock,
A.Kang,
M.L.Land,
R.Levy,
T.J.Lie,
T.A.Major,
B.C.Moore,
I.Porat,
A.Palmeiri,
G.Rouse,
C.Saenphimmachak,
D.Söll,
S.Van Dien,
T.Wang,
W.B.Whitman,
Q.Xia,
Y.Zhang,
F.W.Larimer,
M.V.Olson,
and
J.A.Leigh
(2004).
Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis.
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J Bacteriol,
186,
6956-6969.
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V.Dixit,
E.Bini,
M.Drozda,
and
P.Blum
(2004).
Mercury inactivates transcription and the generalized transcription factor TFB in the archaeon Sulfolobus solfataricus.
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Antimicrob Agents Chemother,
48,
1993-1999.
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J.Zhou,
and
Z.Xu
(2003).
Structural determinants of SecB recognition by SecA in bacterial protein translocation.
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Nat Struct Biol,
10,
942-947.
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PDB code:
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J.H.Laity,
B.M.Lee,
and
P.E.Wright
(2001).
Zinc finger proteins: new insights into structural and functional diversity.
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Curr Opin Struct Biol,
11,
39-46.
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P.R.Mittl,
and
M.G.Grütter
(2001).
Structural genomics: opportunities and challenges.
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Curr Opin Chem Biol,
5,
402-408.
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S.A.Teichmann,
A.G.Murzin,
and
C.Chothia
(2001).
Determination of protein function, evolution and interactions by structural genomics.
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Curr Opin Struct Biol,
11,
354-363.
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S.D.Bell,
and
S.P.Jackson
(2001).
Mechanism and regulation of transcription in archaea.
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Curr Opin Microbiol,
4,
208-213.
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F.Werner,
J.J.Eloranta,
and
R.O.Weinzierl
(2000).
Archaeal RNA polymerase subunits F and P are bona fide homologs of eukaryotic RPB4 and RPB12.
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Nucleic Acids Res,
28,
4299-4305.
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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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}
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