PDBsum entry 1a00

Oxygen transport

PDB id

1a00

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Contents

			Protein chains

					141 a.a. *


					146 a.a. *

			Ligands

					HEM ×4

			Waters ×216

* Residue conservation analysis

PDB id:

1a00

Links

Name:

Oxygen transport

Title:

Hemoglobin (val beta1 met, trp beta37 tyr) mutant

Structure:

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

Source:

Homo sapiens. Human. Organism_taxid: 9606. Organ: blood. Cell: red blood cell. Gene: human beta globin. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Tetramer (from PDB file)

Resolution:

2.00Å

R-factor:

0.169

R-free:

0.223

Authors:

J.S.Kavanaugh,A.Arnone

Key ref:

J.S.Kavanaugh et al. (1998). High-resolution crystal structures of human hemoglobin with mutations at tryptophan 37beta: structural basis for a high-affinity T-state,. Biochemistry, 37, 4358-4373. PubMed id: 9521756 DOI: 10.1021/bi9708702

Date:

08-Dec-97

Release date:

18-Mar-98

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. 146 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 2 residue positions (black crosses)



		Enzyme reactions

Enzyme class:

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

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

DOI no: 10.1021/bi9708702	Biochemistry 37:4358-4373 (1998)
PubMed id: 9521756

High-resolution crystal structures of human hemoglobin with mutations at tryptophan 37beta: structural basis for a high-affinity T-state,.
J.S.Kavanaugh, J.A.Weydert, P.H.Rogers, A.Arnone.

ABSTRACT

The high-resolution X-ray structures of the deoxy forms of four recombinant hemoglobins in which Trp37(C3)beta is replaced with Tyr (betaW37Y), Ala (betaW37A), Glu (betaW37E), or Gly (betaW37G) have been refined and analyzed with superposition methods that partition mutation-induced perturbations into quaternary structure changes and tertiary structure changes. In addition, a new cross-validation statistic that is sensitive to local changes in structure (a "local Rfree" parameter) was used as an objective measure of the significance of the tertiary structure changes. No significant mutation-induced changes in tertiary structure are detected at the mutation site itself for any of the four mutants studied. Instead, disruption of the intersubunit contacts associated with Trp37(C3)beta results in (1) a change in quaternary structure at the alpha1beta2 interface, (2) alpha subunit tertiary structure changes that are centered at Asp94(G1)alpha-Pro95(G2)alpha, (3) beta subunit tertiary structure changes that are located between residues Asp99(G1)beta and Asn102(G4)beta, (4) increased mobility of the alpha subunit COOH-terminal dipeptide, and (5) shortening of the Fe-Nepsilon2His(F8) bond in the alpha and beta subunits of the betaW37G and betaW37E mutants. In each case, the magnitude of the change in a particular structural parameter increases in the order betaW37Y < betaW37A < betaW37E approximately betaW37G, which corresponds closely to the degree of functional disruption documented in the preceding papers.

Literature references that cite this PDB file's key reference

PubMed id

Reference

18083806

J.Guhaniyogi, T.Wu, S.S.Patel, and A.M.Stock (2008).
Interaction of CheY with the C-terminal peptide of CheZ.

J Bacteriol, 190, 1419-1428.

PDB codes:

2pl9 2pmc

15768443

P.Chen, and L.Zhang (2005).
New evidences of glass transitions and microstructures of soy protein plasticized with glycerol.

Macromol Biosci, 5, 237-245.

12023247

L.Mouawad, D.Perahia, C.H.Robert, and C.Guilbert (2002).
New insights into the allosteric mechanism of human hemoglobin from molecular dynamics simulations.

Biophys J, 82, 3224-3245.

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.

11391770

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.

Proteins, 44, 73-78.

11329273

N.R.Naito, H.L.Hui, R.W.Noble, and B.M.Hoffman (2001).
Determination of the hemoglobin surface domains that react with cytochrome b5.

Biochemistry, 40, 2060-2065.

11425320

S.D.Zarić, D.M.Popović, and E.W.Knapp (2001).
Factors determining the orientation of axially coordinated imidazoles in heme proteins.

Biochemistry, 40, 7914-7928.

10681532

B.N.Manjula, A.Malavalli, P.K.Smith, N.L.Chan, A.Arnone, J.M.Friedman, and A.S.Acharya (2000).
Cys-93-betabeta-succinimidophenyl polyethylene glycol 2000 hemoglobin A. Intramolecular cross-bridging of hemoglobin outside the central cavity.

J Biol Chem, 275, 5527-5534.

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.

10790192

R.Li, Y.Nagai, and M.Nagai (2000).
Contribution of alpha140Tyr and beta37Trp to the near-UV CD spectra on quaternary structure transition of human hemoglobin A.

Chirality, 12, 216-220.

9894000

H.L.Hui, J.S.Kavanaugh, M.L.Doyle, A.Wierzba, P.H.Rogers, A.Arnone, J.M.Holt, G.K.Ackers, and R.W.Noble (1999).
Structural and functional properties of human hemoglobins reassembled after synthesis in Escherichia coli.

Biochemistry, 38, 1040-1049.

PDB codes:

1bz1 1bzz

10194373

J.Huang, L.J.Juszczak, E.S.Peterson, C.F.Shannon, M.Yang, S.Huang, G.V.Vidugiris, and J.M.Friedman (1999).
The conformational and dynamic basis for ligand binding reactivity in hemoglobin Ypsilanti (beta 99 asp-->Tyr): origin of the quaternary enhancement effect.

Biochemistry, 38, 4514-4525.

10521410

L.J.Juszczak, and J.M.Friedman (1999).
UV resonance raman spectra of ligand binding intermediates of sol-gel encapsulated hemoglobin.

J Biol Chem, 274, 30357-30360.

9930984

M.Nagai, H.Wajcman, A.Lahary, T.Nakatsukasa, S.Nagatomo, and T.Kitagawa (1999).
Quaternary structure sensitive tyrosine residues in human hemoglobin: UV resonance raman studies of mutants at alpha140, beta35, and beta145 tyrosine.

Biochemistry, 38, 1243-1251.

9521755

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.

Biochemistry, 37, 4346-4357.

9521753

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.

Biochemistry, 37, 4325-4335.

9843411

N.L.Chan, P.H.Rogers, and A.Arnone (1998).
Crystal structure of the S-nitroso form of liganded human hemoglobin.

Biochemistry, 37, 16459-16464.

PDB code:

1buw

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.