1ut0 | pdb_00001ut0
|
CRYSTAL STRUCTURE OF CYTOGLOBIN: THE FOURTH GLOBIN TYPE DISCOVERED IN MAN DISPLAYS HEME HEXA-COORDINATION
Overview
Cytoglobin is a recently discovered hemeprotein belonging to the globin, superfamily together with hemoglobin, myoglobin and neuroglobin. Although, distributed in almost all human tissues, cytoglobin has not been ascribed, a specific function. Human cytoglobin is composed of 190 amino acid, residues. Sequence alignments show that a protein core region (about 150, residues) is structurally related to hemoglobin and myoglobin, being, complemented by about 20 extra residues both on the N and C termini. In, the absence of exogenous ligands (e.g. O2), the cytoglobin distal HisE7, residue is coordinated to the heme Fe atom, thus decreasing the ligand, affinity. The crystal structure of human cytoglobin (2.1 A resolution, 21.3% R-factor) highlights a three-over-three alpha-helical globin fold, ... [(full description)]
About this Structure
1UT0 is a [Single protein] structure of sequence from [Homo sapiens] with HEM and FC6 as [ligands]. Full crystallographic information is available from [OCA].
Reference
Crystal structure of cytoglobin: the fourth globin type discovered in man displays heme hexa-coordination., de Sanctis D, Dewilde S, Pesce A, Moens L, Ascenzi P, Hankeln T, Burmester T, Bolognesi M, J Mol Biol. 2004 Feb 27;336(4):917-27. PMID:15095869
Page seeded by OCA on Mon Oct 29 17:36:35 2007
