PDBsum entry 1bje

Oxygen transport

PDB id

1bje

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Contents

			Protein chain

					153 a.a. *

			Ligands

					SO4


					AZI-HEM

			Waters ×46

* Residue conservation analysis

PDB id:

1bje

Links

Name:

Oxygen transport

Title:

H64t variant of myoglobin (horse heart) recombinant wild-type complexed with azide

Structure:

Myoglobin. Chain: a. Engineered: yes. Mutation: yes

Source:

Equus caballus. Horse. Organism_taxid: 9796. Organ: heart. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.80Å

R-factor:

0.178

Authors:

R.Maurus,G.D.Brayer

Key ref:

R.Maurus et al. (1998). Structural and spectroscopic studies of azide complexes of horse heart myoglobin and the His-64-->Thr variant. Biochem J, 332, 67-74. PubMed id: 9576852

Date:

18-Oct-97

Release date:

28-Jan-98

PROCHECK

	Headers

	References

Protein chain

P68082 (MYG_HORSE) - Myoglobin from Equus caballus

Seq: Struc:					154 a.a. 153 a.a.*

Key:

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 1 residue position (black cross)



		Enzyme reactions

Enzyme class 2:

E.C.1.11.1.- - ?????

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

Enzyme class 3:

E.C.1.7.-.-

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

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

	Biochem J 332:67-74 (1998)
PubMed id: 9576852

Structural and spectroscopic studies of azide complexes of horse heart myoglobin and the His-64-->Thr variant.
R.Maurus, R.Bogumil, N.T.Nguyen, A.G.Mauk, G.Brayer.

ABSTRACT

The high-resolution X-ray crystallographic structures of horse heart azidometmyoglobin complexes of the wild-type protein and the His-64-->Thr variant have been determined to 2.0 and 1.8 A respectively. Azide binds to wild-type metmyoglobin in a bent configuration with an Fe-N-1-N-3 angle of 119 degrees and is oriented into the distal crevice in the direction of Ile-107. The proximity of the His-64 NE2 atom to the N-1 atom of the bound azide indicates stabilization of the ligand by the His-64 side chain through hydrogen bonding. In addition, structural characterization of wild-type horse heart azidometmyoglobin establishes that the only structural change induced by ligand binding is a small movement of the Leu-29 side chain away from the azide ligand. EPR and Fourier transform infrared spectroscopy were used to characterize the myoglobin azide complexes further. EPR spectroscopy revealed that, in contrast with wild-type azidometmyoglobin, two slightly different low-spin species are formed by azide bound to the His-64-->Thr variant both in solution and in a polycrystalline sample. One of these low-spin species has a greater relative intensity, with g values very similar to those of the azide complex of the wild-type protein. These EPR results together with structural information on this variant indicate the presence of two distinct conformations of bound azide, with one form predominating. The major conformation is comparable to that formed by wild-type myoglobin in which azide is oriented into the distal crevice. In the minor conformation the azide is oriented towards the exterior of the protein.

Literature references that cite this PDB file's key reference

PubMed id

Reference

18775958

D.Ulyanov, B.E.Bowler, G.R.Eaton, and S.S.Eaton (2008).
Electron-electron distances in spin-labeled low-spin metmyoglobin variants by relaxation enhancement.

Biophys J, 95, 5306-5316.

18805932

I.B.Cooper, and B.A.Barry (2008).
Azide as a probe of proton transfer reactions in photosynthetic oxygen evolution.

Biophys J, 95, 5843-5850.

17905436

Z.N.Zahran, L.Chooback, D.M.Copeland, A.H.West, and G.B.Richter-Addo (2008).
Crystal structures of manganese- and cobalt-substituted myoglobin in complex with NO and nitrite reveal unusual ligand conformations.

J Inorg Biochem, 102, 216-233.

PDB codes:

2o58 2o5b 2o5l 2o5m 2o5o 2o5q 2o5s 2o5t

17496043

G.De Sanctis, G.Petrella, C.Ciaccio, A.Feis, G.Smulevich, and M.Coletta (2007).
A comparative study on axial coordination and ligand binding in ferric mini myoglobin and horse heart myoglobin.

Biophys J, 93, 2135-2142.

14556636

I.T.Suydam, and S.G.Boxer (2003).
Vibrational Stark effects calibrate the sensitivity of vibrational probes for electric fields in proteins.

Biochemistry, 42, 12050-12055.

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

9860966

M.Lim, P.Hamm, and R.M.Hochstrasser (1998).
Protein fluctuations are sensed by stimulated infrared echoes of the vibrations of carbon monoxide and azide probes.

Proc Natl Acad Sci U S A, 95, 15315-15320.

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.