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PDBsum entry 1a45
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Eye lens protein
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PDB id
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1a45
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Contents |
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* Residue conservation analysis
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PDB id:
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| Name: |
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Eye lens protein
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Title:
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Gammaf crystallin from bovine lens
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Structure:
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Gammaf crystallin. Chain: a
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Source:
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Bos taurus. Cattle. Organism_taxid: 9913. Organ: lens
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Resolution:
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Authors:
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B.V.Norledge,R.Hay,O.A.Bateman,C.Slingsby,H.E.White,D.S.Moss, P.F.Lindley,H.P.C.Driessen
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Key ref:
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B.V.Norledge
et al.
(1997).
Towards a molecular understanding of phase separation in the lens: a comparison of the X-ray structures of two high Tc gamma-crystallins, gammaE and gammaF, with two low Tc gamma-crystallins, gammaB and gammaD.
Exp Eye Res,
65,
609-630.
PubMed id:
DOI:
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Date:
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10-Feb-98
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Release date:
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17-Jun-98
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Supersedes:
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PROCHECK
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Headers
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References
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P23005
(CRGF_BOVIN) -
Gamma-crystallin F from Bos taurus
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Seq:
Struc:
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174 a.a.
173 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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DOI no:
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Exp Eye Res
65:609-630
(1997)
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PubMed id:
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Towards a molecular understanding of phase separation in the lens: a comparison of the X-ray structures of two high Tc gamma-crystallins, gammaE and gammaF, with two low Tc gamma-crystallins, gammaB and gammaD.
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B.V.Norledge,
R.E.Hay,
O.A.Bateman,
C.Slingsby,
H.P.Driessen.
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ABSTRACT
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gamma-Crystallins, although closely related in sequence, show intriguing
differences in their temperature-dependent interactions: those that have a high
or intermediate Tc for phase separation are cryoproteins whereas low Tc
gamma-crystallins are not. To address the molecular basis of phase separation,
X-ray crystallography has been used to define the structural differences between
high and low Tc gamma-crystallins. A pre-requisite for this study was to clarify
the assignment of bovine gene sequences to bovine gamma-crystallin proteins used
for biophysical measurements. Based on nucleotide sequence analyses of gamma E
and gamma F bovine crystallin genes, gamma F corresponds to the previously
crystallised high Tc protein bovine gamma IVa and gamma E corresponds to the
high Tc bovine protein fraction previously known as gamma IIIa. The gamma F
sequence has enabled the completion of the refinement of the bovine gamma F
crystal structure which shows that the molecule has an additional surface
tryptophan explaining why gamma F has different spectroscopic properties from
gamma B. A high Tc protein from rat lens, gamma E crystallin, has been
crystallised and the X-ray structure solved at 2.3 A resolution. Comparison of
the X-ray structures of two high Tc proteins, rat gamma E and bovine gamma F,
with the structures of two low Tc proteins, bovine gamma B and bovine gamma D,
shows that the main conformational change between high and low Tc proteins is in
the cd surface loop of motif 3. All four structures have numerous ion pairs on
their surfaces leading to a high surface charge density, yet with low overall
charge. Comparison of the lattice contacts of the two high Tc proteins with the
two low Tc gamma-crystallins indicates that these high Tc proteins utilise more
amino-aromatic interactions such as between histidine and arginine. Comparison
of the sequences of all the gamma-crystallins which have been characterised for
phase separation temperature indicates that only residue Arg/Lys 163 uniquely
distinguishes cryo from non-cryo gamma-crystallins and it is close to the
altered surface loop. Although this region probably contributes to phase
separation, Tc is likely to be a function of an overall global property that is
responsive to overall charge distribution. Calculated dipole moments of native
gamma-crystallins, low Tc gamma-crystallin sequences threaded into high Tc
gamma-crystallin structures, and vice versa, show how both sequence and 3D
structure contribute to this overall property. High Tc gamma-crystallins have on
average higher Arg/Lys ratios and higher histidine content. It is hypothesised
that this increases the proportion of surface static paired charged networks
which thus reduces the repulsive hydration force and so increases the attractive
interactions of the protein-rich phase in binary liquid phase separation.
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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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S.Lee,
B.Mahler,
J.Toward,
B.Jones,
K.Wyatt,
L.Dong,
G.Wistow,
and
Z.Wu
(2010).
A single destabilizing mutation (F9S) promotes concerted unfolding of an entire globular domain in gammaS-crystallin.
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J Mol Biol,
399,
320-330.
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C.J.Weadick,
and
B.S.Chang
(2009).
Molecular evolution of the betagamma lens crystallin superfamily: evidence for a retained ancestral function in gamma N crystallins?
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Mol Biol Evol,
26,
1127-1142.
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J.Chen,
P.R.Callis,
and
J.King
(2009).
Mechanism of the very efficient quenching of tryptophan fluorescence in human gammaD- and gammaS-crystallins: the gamma-crystallin fold may have evolved to protect tryptophan residues from ultraviolet photodamage.
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Biochemistry,
48,
3708-3716.
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N.Volkmann
(2009).
Confidence intervals for fitting of atomic models into low-resolution densities.
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Acta Crystallogr D Biol Crystallogr,
65,
679-689.
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A.G.Purkiss,
O.A.Bateman,
K.Wyatt,
P.A.Wilmarth,
L.L.David,
G.J.Wistow,
and
C.Slingsby
(2007).
Biophysical properties of gammaC-crystallin in human and mouse eye lens: the role of molecular dipoles.
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J Mol Biol,
372,
205-222.
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PDB code:
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J.B.Artero,
M.Härtlein,
S.McSweeney,
and
P.Timmins
(2005).
A comparison of refined X-ray structures of hydrogenated and perdeuterated rat gammaE-crystallin in H2O and D2O.
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Acta Crystallogr D Biol Crystallogr,
61,
1541-1549.
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PDB codes:
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Z.Wu,
F.Delaglio,
K.Wyatt,
G.Wistow,
and
A.Bax
(2005).
Solution structure of (gamma)S-crystallin by molecular fragment replacement NMR.
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Protein Sci,
14,
3101-3114.
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PDB codes:
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M.S.Kosinski-Collins,
and
J.King
(2003).
In vitro unfolding, refolding, and polymerization of human gammaD crystallin, a protein involved in cataract formation.
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Protein Sci,
12,
480-490.
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A.G.Purkiss,
O.A.Bateman,
J.M.Goodfellow,
N.H.Lubsen,
and
C.Slingsby
(2002).
The X-ray crystal structure of human gamma S-crystallin C-terminal domain.
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J Biol Chem,
277,
4199-4205.
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PDB code:
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M.H.Seto,
H.L.Liu,
D.A.Zajchowski,
and
M.Whitlow
(1999).
Protein fold analysis of the B30.2-like domain.
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Proteins,
35,
235-249.
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S.Palme,
R.Jaenicke,
and
C.Slingsby
(1998).
X-ray structures of three interface mutants of gammaB-crystallin from bovine eye lens.
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Protein Sci,
7,
611-618.
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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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Links
