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PDBsum entry 1gli
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Oxygen transport
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PDB id
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1gli
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Contents |
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* Residue conservation analysis
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Enzyme class:
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Chains A, B, C, D:
E.C.?
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J Biol Chem
271:12472-12480
(1996)
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PubMed id:
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Probing the alpha 1 beta 2 interface of human hemoglobin by mutagenesis. Role of the FG-C contact regions.
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B.Vallone,
A.Bellelli,
A.E.Miele,
M.Brunori,
G.Fermi.
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ABSTRACT
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The allosteric transition of hemoglobin involves an extensive reorganization of
the alpha 1 beta 2 interface, in which two contact regions have been identified.
This paper concerns at the effect of two mutations located in the "switch"
(alpha C3 Thr --> Trp) and the "flexible joint" (beta C3 Trp --> Thr). We
have expressed and characterized one double and two single mutants: Hb alpha
T38W/beta W37T, Hb beta W37T, and Hb alpha T38W, whose structure has been
determined by crystallography. We present data on: (i) the interface structure
in the contact regions, (ii) oxygen and CO binding kinetics and cooperativity,
(iii) dissociation rates of deoxy tetramers and association rates of deoxy
dimers, and (iv) the effect of NaI on deoxy tetramer dissociation rate constant.
All the mutants are tetrameric and T-state in the deoxygenated derivative.
Reassociation of deoxygenated dimers is not modified by interface mutations.
DeoxyHb alpha T38W/beta W37T dissociate much faster. We propose a binding site
for I- at the switch region. The single mutants binds O2 cooperatively; the
double one is almost non-cooperative, a feature confirmed by CO binding. The
functional data, analyzed with the two-state model, indicate that these
mutations reduce the value of the allosteric constant LO.
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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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M.R.Mihailescu,
C.Fronticelli,
and
I.M.Russu
(2001).
Allosteric free energy changes at the alpha 1 beta 2 interface of human hemoglobin probed by proton exchange of Trp beta 37.
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Proteins,
44,
73-78.
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J.C.Burnett,
G.E.Kellogg,
and
D.J.Abraham
(2000).
Computational methodology for estimating changes in free energies of biomolecular association upon mutation. The importance of bound water in dimer-tetramer assembly for beta 37 mutant hemoglobins.
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Biochemistry,
39,
1622-1633.
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E.S.Peterson,
and
J.M.Friedman
(1998).
A possible allosteric communication pathway identified through a resonance Raman study of four beta37 mutants of human hemoglobin A.
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Biochemistry,
37,
4346-4357.
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L.D.Kwiatkowski,
H.L.Hui,
A.Wierzba,
R.W.Noble,
R.Y.Walder,
E.S.Peterson,
S.G.Sligar,
and
K.E.Sanders
(1998).
Preparation and kinetic characterization of a series of betaW37 variants of human hemoglobin A: evidence for high-affinity T quaternary structures.
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Biochemistry,
37,
4325-4335.
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L.Kiger,
A.L.Klinger,
L.D.Kwiatkowski,
A.De Young,
M.L.Doyle,
J.M.Holt,
R.W.Noble,
and
G.K.Ackers
(1998).
Thermodynamic studies on the equilibrium properties of a series of recombinant betaW37 hemoglobin mutants.
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Biochemistry,
37,
4336-4345.
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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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Links
