PDBsum entry 1dxt

Oxygen transport

PDB id

1dxt

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Contents

			Protein chains

					141 a.a. *


					147 a.a. *

			Ligands

					HEM ×4

			Waters ×227

* Residue conservation analysis

PDB id:

1dxt

Links

Name:

Oxygen transport

Title:

High-resolution x-ray study of deoxy recombinant human hemoglobins synthesized from beta-globins having mutated amino termini

Structure:

Hemoglobin (deoxy) (alpha chain). Chain: a, c. Engineered: yes. Hemoglobin (deoxy) (beta chain). Chain: b, d. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_taxid: 562

Biol. unit:

Tetramer (from PQS)

Resolution:

1.70Å

R-factor:

0.160

Authors:

J.S.Kavanaugh,A.Arnone

Key ref:

J.S.Kavanaugh et al. (1992). High-resolution X-ray study of deoxy recombinant human hemoglobins synthesized from beta-globins having mutated amino termini. Biochemistry, 31, 8640-8647. PubMed id: 1390648 DOI: 10.1021/bi00151a034

Date:

06-May-92

Release date:

31-Oct-93

PROCHECK

	Headers

	References

Protein chains

P69905 (HBA_HUMAN) - Hemoglobin subunit alpha from Homo sapiens

Seq: Struc:					142 a.a. 141 a.a.

Protein chains

P68871 (HBB_HUMAN) - Hemoglobin subunit beta from Homo sapiens

Seq: Struc:					147 a.a. 147 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

Chains A, B, C, D: E.C.?

[IntEnz] [ExPASy] [KEGG] [BRENDA]

DOI no: 10.1021/bi00151a034	Biochemistry 31:8640-8647 (1992)
PubMed id: 1390648

High-resolution X-ray study of deoxy recombinant human hemoglobins synthesized from beta-globins having mutated amino termini.
J.S.Kavanaugh, P.H.Rogers, A.Arnone.

ABSTRACT

The crystal structures of three mutant hemoglobins reconstituted from recombinant beta chains and authentic human alpha chains have been determined in the deoxy state at 1.8-A resolution. The primary structures of the mutant hemoglobins differ at the beta-chain amino terminus. One mutant, beta Met, is characterized by the addition of a methionine at the amino terminus. The other two hemoglobins are characterized by substitution of Val 1 beta with either a methionine, beta V1M, or an alanine, beta V1A. All the mutation-induced structural perturbations are small intrasubunit changes that are localized to the immediate vicinity of the beta-chain amino terminus. In the beta Met and beta V1A mutants, the mobility of the beta-chain amino terminus increases and the electron density of an associated inorganic anion is decreased. In contrast, the beta-chain amino terminus of the beta V1M mutant becomes less mobile, and the inorganic anion binds with increased affinity. These structural differences can be correlated with functional data for the mutant hemoglobins [Doyle, M. L., Lew, G., DeYoung, A., Kwiatkowski, L., Noble, R. W., & Ackers, G. K. (1992) Biochemistry preceding paper is this issue] as well as with the properties of ruminant hemoglobins and a mechanism [Perutz, M., & Imai, K. (1980) J. Mol. Biol. 136, 183-191] that relates the intrasubunit interactions of the beta-chain amino terminus to changes in oxygen affinity. Since the structures of the mutant deoxyhemoglobins show only subtle differences from the structure of deoxyhemoglobin A, it is concluded that any of the three hemoglobins could probably function as a surrogate for hemoglobin A.(ABSTRACT TRUNCATED AT 250 WORDS)

Literature references that cite this PDB file's key reference

PubMed id

Reference

15495251

O.Abdulmalik, M.K.Safo, N.B.Lerner, J.Ochotorena, E.Daikhin, V.Lakka, R.Santacroce, D.J.Abraham, and T.Asakura (2004).
Characterization of hemoglobin bassett (alpha94Asp-->Ala), a variant with very low oxygen affinity.

Am J Hematol, 77, 268-276.

PDB codes:

1r1x 1r1y

11514675

J.S.Kavanaugh, J.A.Weydert, P.H.Rogers, A.Arnone, H.L.Hui, A.M.Wierzba, L.D.Kwiatkowski, P.Paily, R.W.Noble, S.Bruno, and A.Mozzarelli (2001).
Site-directed mutations of human hemoglobin at residue 35beta: a residue at the intersection of the alpha1beta1, alpha1beta2, and alpha1alpha2 interfaces.

Protein Sci, 10, 1847-1855.

11514664

R.D.Kidd, H.M.Baker, A.J.Mathews, T.Brittain, and E.N.Baker (2001).
Oligomerization and ligand binding in a homotetrameric hemoglobin: two high-resolution crystal structures of hemoglobin Bart's (gamma(4)), a marker for alpha-thalassemia.

Protein Sci, 10, 1739-1749.

PDB codes:

1i3d 1i3e

11076511

C.H.Tsai, T.Y.Fang, N.T.Ho, and C.Ho (2000).
Novel recombinant hemoglobin, rHb (beta N108Q), with low oxygen affinity, high cooperativity, and stability against autoxidation.

Biochemistry, 39, 13719-13729.

10930828

E.A.Brucker (2000).
Genetically crosslinked hemoglobin: a structural study.

Acta Crystallogr D Biol Crystallogr, 56, 812-816.

PDB codes:

1c7b 1c7c 1c7d

10677211

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.

Biochemistry, 39, 1622-1633.

10716987

J.M.Nocek, K.Huang, and B.M.Hoffman (2000).
Extension of transverse relaxation-optimized spectroscopy techniques to allosteric proteins: CO- and paramagnetic fluoromet-hemoglobin [beta (15N-valine)].

Proc Natl Acad Sci U S A, 97, 2538-2543.

10930827

J.R.Tame, and B.Vallone (2000).
The structures of deoxy human haemoglobin and the mutant Hb Tyralpha42His at 120 K.

Acta Crystallogr D Biol Crystallogr, 56, 805-811.

PDB codes:

1a3n 1a3o

9649306

Y.A.Puius, M.Zou, N.T.Ho, C.Ho, and S.C.Almo (1998).
Novel water-mediated hydrogen bonds as the structural basis for the low oxygen affinity of the blood substitute candidate rHb(alpha 96Val-->Trp).

Biochemistry, 37, 9258-9265.

PDB codes:

1rvw 1vwt

9032082

K.S.Kroeger, and C.E.Kundrot (1997).
Structures of a hemoglobin-based blood substitute: insights into the function of allosteric proteins.

Structure, 5, 227-237.

PDB codes:

1abw 1aby

9407091

S.Bettati, L.D.Kwiatkowski, J.S.Kavanaugh, A.Mozzarelli, A.Arnone, G.L.Rossi, and R.W.Noble (1997).
Structure and oxygen affinity of crystalline des-his-146beta human hemoglobin in the T state.

J Biol Chem, 272, 33077-33084.

PDB code:

1axf

8647854

B.Vallone, A.Bellelli, A.E.Miele, M.Brunori, and G.Fermi (1996).
Probing the alpha 1 beta 2 interface of human hemoglobin by mutagenesis. Role of the FG-C contact regions.

J Biol Chem, 271, 12472-12480.

PDB code:

1gli

8639677

I.Pechik, X.Ji, K.Fidelis, M.Karavitis, J.Moult, W.S.Brinigar, C.Fronticelli, and G.L.Gilliland (1996).
Crystallographic, molecular modeling, and biophysical characterization of the valine beta 67 (E11)-->threonine variant of hemoglobin.

Biochemistry, 35, 1935-1945.

PDB codes:

1hdb 2hhd

8840785

S.C.Makrides (1996).
Strategies for achieving high-level expression of genes in Escherichia coli.

Microbiol Rev, 60, 512-538.

7592833

R.A.Hernan, and S.G.Sligar (1995).
Tetrameric hemoglobin expressed in Escherichia coli. Evidence of heterogeneous subunit assembly.

J Biol Chem, 270, 26257-26264.

8430105

J.J.Martin de Llano, O.Schneewind, G.Stetler, and J.M.Manning (1993).
Recombinant human sickle hemoglobin expressed in yeast.

Proc Natl Acad Sci U S A, 90, 918-922.

8367471

T.J.Shen, N.T.Ho, V.Simplaceanu, M.Zou, B.N.Green, M.F.Tam, and C.Ho (1993).
Production of unmodified human adult hemoglobin in Escherichia coli.

Proc Natl Acad Sci U S A, 90, 8108-8112.

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.