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.

Makino M, Sugimoto H, Sawai H, Kawada N, Yoshizato K, Shiro Y.

Source

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; [PubMed - indexed for MEDLINE]

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Cited by 2 PubMed Central articles

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Structures reported by this article

Crystal Structure Of Human Cytoglobin At 1.68 Angstroms Resolution

PDB: 2DC3

Source: Homo sapiens

Method: X-Ray Diffraction

Resolution: 1.68 Å

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