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* Residue conservation analysis
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DOI no:
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Biochemistry
39:15353-15364
(2000)
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PubMed id:
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Interface sliding as illustrated by the multiple quaternary structures of liganded hemoglobin.
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T.C.Mueser,
P.H.Rogers,
A.Arnone.
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ABSTRACT
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Initial crystallographic studies suggested that fully liganded mammalian
hemoglobin can adopt only a single quaternary structure, the quaternary R
structure. However, more recent crystallographic studies revealed the existence
of a second quaternary structure for liganded hemoglobin, the quaternary R2
structure. Since these quaternary structures can be crystallized, both must be
energetically accessible structures that coexist in solution. Unanswered
questions include (i) the relative abundance of the R and R2 structures under
various solution conditions and (ii) whether other quaternary structures are
energetically accessible for the liganded alpha(2)beta(2) hemoglobin tetramer.
Although crystallographic methods cannot directly answer the first question,
they represent the most direct and most accurate approach to answering the
second question. We now have determined and refined three different crystal
structures of bovine carbonmonoxyhemoglobin. These structures provide clear
evidence that the dimer-dimer interface of liganded hemoglobin has a wide range
of energetically accessible structures that are related to each other by a
simple sliding motion. The dimer-dimer interface acts as a "molecular slide
bearing" that allows the two alpha beta dimers to slide back and forth without
greatly altering the number or the nature of the intersubunit contacts. Since
the general stereochemical features of this interface are not unusual, it is
likely that interface sliding of the kind displayed by fully liganded hemoglobin
plays important structural and functional roles in many other protein assemblies.
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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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PDB codes:
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PDB code:
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PDB codes:
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X.Hong,
and
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(2009).
Measurements of accurate x-ray scattering data of protein solutions using small stationary sample cells.
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Kinetic-dynamic model for conformational control of an electron transfer photocycle: mixed-metal hemoglobin hybrids.
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J Phys Chem B,
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C.Ciaccio,
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and
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(2008).
Cooperativity and allostery in haemoglobin function.
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IUBMB Life,
60,
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P.S.Kaushal,
R.Sankaranarayanan,
and
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(2008).
Water-mediated variability in the structure of relaxed-state haemoglobin.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
64,
463-469.
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PDB codes:
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T.Yonetani,
and
M.Laberge
(2008).
Protein dynamics explain the allosteric behaviors of hemoglobin.
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Biochim Biophys Acta,
1784,
1146-1158.
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X.J.Song,
V.Simplaceanu,
N.T.Ho,
and
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(2008).
Effector-induced structural fluctuation regulates the ligand affinity of an allosteric protein: binding of inositol hexaphosphate has distinct dynamic consequences for the T and R states of hemoglobin.
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Biochemistry,
47,
4907-4915.
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Y.Zhang,
V.S.Bhatt,
G.Sun,
P.G.Wang,
and
A.F.Palmer
(2008).
Site-selective glycosylation of hemoglobin on Cys beta93.
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Bioconjug Chem,
19,
2221-2230.
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B.L.Boys,
and
L.Konermann
(2007).
Folding and assembly of hemoglobin monitored by electrospray mass spectrometry using an on-line dialysis system.
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J Am Soc Mass Spectrom,
18,
8.
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K.Neelagandan,
P.S.Moorthy,
M.Balasubramanian,
and
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(2007).
Crystallization of sheep (Ovis aries) and goat (Capra hircus) haemoglobins under unbuffered low-salt conditions.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
63,
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S.C.Sahu,
V.Simplaceanu,
Q.Gong,
N.T.Ho,
F.Tian,
J.H.Prestegard,
and
C.Ho
(2007).
Insights into the solution structure of human deoxyhemoglobin in the absence and presence of an allosteric effector.
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Biochemistry,
46,
9973-9980.
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X.J.Song,
Y.Yuan,
V.Simplaceanu,
S.C.Sahu,
N.T.Ho,
and
C.Ho
(2007).
A comparative NMR study of the polypeptide backbone dynamics of hemoglobin in the deoxy and carbonmonoxy forms.
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Biochemistry,
46,
6795-6803.
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A.Izaac,
C.A.Schall,
and
T.C.Mueser
(2006).
Assessment of a preliminary solubility screen to improve crystallization trials: uncoupling crystal condition searches.
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Acta Crystallogr D Biol Crystallogr,
62,
833-842.
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C.J.Roche,
D.Dantsker,
U.Samuni,
and
J.M.Friedman
(2006).
Nitrite reductase activity of sol-gel-encapsulated deoxyhemoglobin. Influence of quaternary and tertiary structure.
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J Biol Chem,
281,
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H.X.Zhou
(2005).
Interactions of macromolecules with salt ions: an electrostatic theory for the Hofmeister effect.
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Proteins,
61,
69-78.
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K.Victor,
A.Van-Quynh,
and
R.G.Bryant
(2005).
High frequency dynamics in hemoglobin measured by magnetic relaxation dispersion.
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Biophys J,
88,
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L.N.Patskovska,
Y.V.Patskovsky,
S.C.Almo,
and
R.E.Hirsch
(2005).
COHbC and COHbS crystallize in the R2 quaternary state at neutral pH in the presence of PEG 4000.
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Acta Crystallogr D Biol Crystallogr,
61,
566-573.
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PDB codes:
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R.Sankaranarayanan,
B.K.Biswal,
and
M.Vijayan
(2005).
A new relaxed state in horse methemoglobin characterized by crystallographic studies.
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Proteins,
60,
547-551.
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PDB codes:
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S.V.Lepeshkevich,
and
B.M.Dzhagarov
(2005).
Mutual effects of proton and sodium chloride on oxygenation of liganded human hemoglobin.
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FEBS J,
272,
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B.K.Collins,
S.J.Tomanicek,
N.Lyamicheva,
M.W.Kaiser,
and
T.C.Mueser
(2004).
A preliminary solubility screen used to improve crystallization trials: crystallization and preliminary X-ray structure determination of Aeropyrum pernix flap endonuclease-1.
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Acta Crystallogr D Biol Crystallogr,
60,
1674-1678.
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V.Baudin-Creuza,
C.Vasseur-Godbillon,
C.Pato,
C.Préhu,
H.Wajcman,
and
M.C.Marden
(2004).
Transfer of human alpha- to beta-hemoglobin via its chaperone protein: evidence for a new state.
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J Biol Chem,
279,
36530-36533.
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Y.Zheng,
J.L.Giovannelli,
N.T.Ho,
C.Ho,
and
D.Yang
(2004).
Side-chain assignments of methyl-containing residues in a uniformly 13C-labeled hemoglobin in the carbonmonoxy form.
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J Biomol NMR,
30,
423-429.
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A.G.Salvay,
J.R.Grigera,
and
M.F.Colombo
(2003).
The role of hydration on the mechanism of allosteric regulation: in situ measurements of the oxygen-linked kinetics of water binding to hemoglobin.
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Biophys J,
84,
564-570.
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J.A.Lukin,
G.Kontaxis,
V.Simplaceanu,
Y.Yuan,
A.Bax,
and
C.Ho
(2003).
Quaternary structure of hemoglobin in solution.
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Proc Natl Acad Sci U S A,
100,
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A.Riccio,
L.Vitagliano,
G.di Prisco,
A.Zagari,
and
L.Mazzarella
(2002).
The crystal structure of a tetrameric hemoglobin in a partial hemichrome state.
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Proc Natl Acad Sci U S A,
99,
9801-9806.
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PDB code:
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B.K.Biswal,
and
M.Vijayan
(2002).
Structures of human oxy- and deoxyhaemoglobin at different levels of humidity: variability in the T state.
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Acta Crystallogr D Biol Crystallogr,
58,
1155-1161.
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PDB codes:
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L.Mouawad,
D.Perahia,
C.H.Robert,
and
C.Guilbert
(2002).
New insights into the allosteric mechanism of human hemoglobin from molecular dynamics simulations.
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Biophys J,
82,
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N.Shibayama,
S.Miura,
J.R.Tame,
T.Yonetani,
and
S.Y.Park
(2002).
Crystal structure of horse carbonmonoxyhemoglobin-bezafibrate complex at 1.55-A resolution. A novel allosteric binding site in R-state hemoglobin.
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J Biol Chem,
277,
38791-38796.
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PDB code:
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U.Samuni,
D.Dantsker,
I.Khan,
A.J.Friedman,
E.Peterson,
and
J.M.Friedman
(2002).
Spectroscopically and kinetically distinct conformational populations of sol-gel-encapsulated carbonmonoxy myoglobin. A comparison with hemoglobin.
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J Biol Chem,
277,
25783-25790.
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A.Riccio,
L.Vitagliano,
G.di Prisco,
A.Zagari,
and
L.Mazzarella
(2001).
Liganded and unliganded forms of Antarctic fish haemoglobins in polyethylene glycol: crystallization of an R-state haemichrome intermediate.
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Acta Crystallogr D Biol Crystallogr,
57,
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W.E.Royer,
J.E.Knapp,
K.Strand,
and
H.A.Heaslet
(2001).
Cooperative hemoglobins: conserved fold, diverse quaternary assemblies and allosteric mechanisms.
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Trends Biochem Sci,
26,
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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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