Format

Send to

Choose Destination
Acta Crystallogr D Biol Crystallogr. 2006 Jun;62(Pt 6):671-7. Epub 2006 May 12.

High-resolution structure of human cytoglobin: identification of extra N- and C-termini and a new dimerization mode.

Author information

1
Biometal Science Laboratory, Harima Institute, RIKEN SPring-8 Center, Harima Institute, Japan.

Abstract

Cytoglobin (Cgb) is a recently discovered member of the vertebrate haem-containing globin family. The structure of a new crystal form of wild-type human Cgb (space group C2) was determined at a resolution of 1.68 Angstrom. The results show the presence of an additional helix in the N-terminal residues (4-20) prior to the A helix and an ordered loop structure in the C-terminal region (168-188), while these extended peptides were invisible owing to disorder in the previously reported structures using a P3(2)21 crystal at a resolution of 2.4 Angstrom. A detailed comparison of the two crystal structures shows differences in the conformation of the residues (i.e. Arg84) in the haem environment owing to a different dimeric arrangement.

PMID:
16699195
DOI:
10.1107/S0907444906013813
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for International Union of Crystallography
Loading ...
Support Center