PDBsum entry 1myt

Oxygen transport

PDB id

1myt

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Contents

			Protein chain

					146 a.a. *

			Ligands

					HEM

			Waters ×81

* Residue conservation analysis

PDB id:

1myt

Links

Name:

Oxygen transport

Title:

Crystal structure to 1.74 angstroms resolution of metmyoglobin from yellowfin tuna (thunnus albacares): an example of a myoglobin lacking the d helix

Structure:

Myoglobin. Chain: a. Engineered: yes

Source:

Thunnus albacares. Yellowfin tuna. Organism_taxid: 8236

Resolution:

1.74Å

R-factor:

0.177

Authors:

G.I.Birnbaum,S.V.Evans,M.Przybylska,D.R.Rose

Key ref:

G.I.Birnbaum et al. (1994). 1.70 A resolution structure of myoglobin from yellowfin tuna. An example of a myoglobin lacking the D helix. Acta Crystallogr D Biol Crystallogr, 50, 283-289. PubMed id: 15299440 DOI: 10.1107/S0907444993014271

Date:

06-May-91

Release date:

31-Oct-93

PROCHECK

	Headers

	References

Protein chain

P02205 (MYG_THUAL) - Myoglobin from Thunnus albacares

Seq: Struc:					147 a.a. 146 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.?

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

DOI no: 10.1107/S0907444993014271	Acta Crystallogr D Biol Crystallogr 50:283-289 (1994)
PubMed id: 15299440

1.70 A resolution structure of myoglobin from yellowfin tuna. An example of a myoglobin lacking the D helix.
G.I.Birnbaum, S.V.Evans, M.Przybylska, D.R.Rose.

ABSTRACT

The crystal structure of metmyoglobin from yellowfin tuna (Thunnus albacares) has been determined by molecular replacement methods and refined to a conventional R factor of 0.177 for all observed reflections in the range of 6.0-1.70 A resolution. Like other myoglobins for which a high-resolution structure is available, the polypeptide chain is organized into several helices that cooperate to form a hydrophobic pocket into which the heme prosthetic group is non-covalently bound; however, the D helix observed in other myoglobins is absent in myoglobin from yellowfin tuna and has been replaced with a random coil. As well, the A helix has a pronounced kink due to the presence of Pro16. The differences in structure between this and sperm whale myoglobin can be correlated with their reported dioxygen affinity and dissociation. The structure is in agreement with reported fluorescence data which show an increased Trp14.heme distance in yellowfin tuna compared to sperm whale myoglobin.

Selected figure(s)



	Figure 4. Fig. 4. Aignment of the primary sequence of YFT and SW myo- glbin.		Figure 8. Fig. 8. Stereoview of the heme group and its distal an proximal histidine groups, and their corresponding electron dnsity. The heme iron is diplaed by 0.09 A out of the mean plane of the pyrrole N atoms toward the heme ligand His93.

Figures were selected by an automated process.

Literature references that cite this PDB file's key reference

PubMed id

Reference

18618699

E.Bismuto, E.Di Maggio, S.Pleus, M.Sikor, C.Röcker, G.U.Nienhaus, and D.C.Lamb (2009).
Molecular dynamics simulation of the acidic compact state of apomyoglobin from yellowfin tuna.

Proteins, 74, 273-290.

17488722

E.R.Schreiter, M.M.Rodríguez, A.Weichsel, W.R.Montfort, and J.Bonaventura (2007).
S-nitrosylation-induced conformational change in blackfin tuna myoglobin.

J Biol Chem, 282, 19773-19780.

PDB codes:

2nrl 2nrm 2nx0

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.