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PDBsum entry 1ds9
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Contractile protein
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PDB id
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1ds9
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Solution structure of a dynein motor domain associated light chain.
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Authors
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H.Wu,
M.W.Maciejewski,
A.Marintchev,
S.E.Benashski,
G.P.Mullen,
S.M.King.
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Ref.
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Nat Struct Biol, 2000,
7,
575-579.
[DOI no: ]
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PubMed id
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Abstract
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Dyneins are molecular motors that translocate towards the minus ends of
microtubules. In Chlamydomonas flagellar outer arm dynein, light chain 1 (LC1)
associates with the nucleotide binding region within the gamma heavy chain motor
domain and consists of a central leucine-rich repeat section that folds as a
cylindrical right handed spiral formed from six beta-beta-alpha motifs. This
central cylinder is flanked by terminal helical subdomains. The C-terminal
helical domain juts out from the cylinder and is adjacent to a hydrophobic
surface within the repeat region that is proposed to interact with the dynein
heavy chain. The position of the C-terminal domain on LC1 and the unexpected
structural similarity between LC1 and U2A' from the human spliceosome suggest
that this domain interacts with the dynein motor domain.
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Figure 2.
Figure 2. The NMR solution structure of LC1. a, Stereo view
of the backbone trace for a superposition of the 17 lowest
energy LC1 structures is shown. Colors used for the  -helices
and  -strands
correspond to the topology diagram in Fig. 1b. The N-terminus is
at the bottom of the displayed structures. b, Ribbon
representation of the mean LC1 structure with individual
secondary structure elements labeled. c, Superimposition of the
hydrophobic side chains (green) that pack the core of the
leucine rich repeat region are shown on the mean backbone
(orange).
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Figure 3.
Figure 3. Electrostatic surface of LC1 and proposed heavy chain
binding site. a, Two views (related by 90° rotation about the
y-axis) of the electrostatic surface of LC1 are shown. The
hydrophobic patch, which includes Trp 99, Tyr 121 and Leu 146 on
the -sheet
face, is evident in the view on the right. It is this patch that
may be involved in attachment of LC1 to the  heavy
chain. The opposite surface proposed to interact with p45 (left
view) is highly charged, with patches of both acidic and basic
residues. The surface potential was calculated using dielectric
constants of 30 and 80 for protein and solvent, respectively.
The images are oriented with the N-terminus to the top. b, Close
up stereo view of the putative heavy
chain binding surface. Side chains at positions that are
hydrophobic in all family members are shown in green (Trp 99 and
Leu 146), whereas hydrophobic side chains at less conserved
positions are in yellow (Ile 74, Tyr 102, Val 119 and Tyr 121).
Acidic and basic residues that surround the hydrophobic patch
are shown in red and blue, respectively. c, The superimposed
ribbon structures of LC1 (orange) and U2A' (yellow; accession
code 1A9N) are shown to illustrate the structural homology
between these two molecules. The r.m.s. deviation for
superimposed C atoms
is 3.7 Å as determined by DALI (version 2.0)30.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(2000,
7,
575-579)
copyright 2000.
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Secondary reference #1
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Title
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1h, 15n and 13c resonance assignments for the 22 kda lc1 light chain from chlamydomonas outer arm dynein.
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Authors
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H.Wu,
M.W.Maciejewski,
S.E.Benashski,
G.P.Mullen,
S.M.King.
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Ref.
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J Biomol Nmr, 1999,
13,
309-310.
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PubMed id
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