PDBsum entry 1fcs

Oxygen transport

PDB id

1fcs

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Contents

			Protein chain

					154 a.a. *

			Ligands

					SO4 ×2


					HEM

			Waters ×120

* Residue conservation analysis

PDB id:

1fcs

Links

Name:

Oxygen transport

Title:

Crystal structure of a distal site double mutant of sperm whale myoglobin at 1.6 angstroms resolution

Structure:

Myoglobin. Chain: a. Engineered: yes

Source:

Physeter catodon. Sperm whale. Organism_taxid: 9755. Gene: synthetic gene

Resolution:

1.60Å

R-factor:

0.197

Authors:

M.Rizzi,M.Bolognesi,A.Coda,F.Cutruzzola,C.Travaglini Allocatelli, A.Brancaccio,M.Brunori

Key ref:

M.Rizzi et al. (1993). Crystal structure of a distal site double mutant of sperm whale myoglobin at 1.6 A resolution. FEBS Lett, 320, 13-16. PubMed id: 8462669 DOI: 10.1016/0014-5793(93)81647-I

Date:

20-Apr-93

Release date:

31-Oct-93

PROCHECK

	Headers

	References

Protein chain

P02185 (MYG_PHYMC) - Myoglobin from Physeter macrocephalus

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

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 3 residue positions (black crosses)



		Enzyme reactions

Enzyme class:

E.C.?

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

DOI no: 10.1016/0014-5793(93)81647-I	FEBS Lett 320:13-16 (1993)
PubMed id: 8462669

Crystal structure of a distal site double mutant of sperm whale myoglobin at 1.6 A resolution.
M.Rizzi, M.Bolognesi, A.Coda, F.Cutruzzolà, C.T.Allocatelli, A.Brancaccio, M.Brunori.

ABSTRACT

The three-dimensional structure of sperm whale myoglobin His64(E7)-->Val,Thr67(E10)-->Arg double mutant has been studied by X-ray crystallography at 1.6 A resolution, and refined to a crystallographic R-factor of 0.197. The Arg67(E10) side chain is extended in the direction of the ligand binding site, and its NH1 atom is at a distance of 3.11 A from the NH1 atom of Arg45(CD3), which is also pointing towards the distal site. Both are kept in this position by hydrogen bonding and electrostatic interactions with a solvent sulfate ion, located amongst the two, on the protein surface. No liganded water molecule is present at the sixth coordination position of the Fe(III) heme.

Literature references that cite this PDB file's key reference

PubMed id

Reference

8999946

J.A.DeGray, M.R.Gunther, R.Tschirret-Guth, P.R.Ortiz de Montellano, and R.P.Mason (1997).
Peroxidation of a specific tryptophan of metmyoglobin by hydrogen peroxide.

J Biol Chem, 272, 2359-2362.

7656050

X.Huang, and S.G.Boxer (1994).
Discovery of new ligand binding pathways in myoglobin by random mutagenesis.

Nat Struct Biol, 1, 226-229.

8298042

J.Qin, G.N.La Mar, F.Cutruzzolá, C.T.Allocatelli, A.Brancaccio, and M.Brunori (1993).
Solution 1H nuclear magnetic resonance determination of the distal pocket structure of cyanomet complexes of genetically engineered sperm whale myoglobin His64 (E7)-->Val, Thr67 (E10)-->Arg. The role of distal hydrogen bonding by Arg67 (E10) in modulating ligand tilt.

Biophys J, 65, 2178-2190.

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.