1kr7

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Revision as of 11:05, 8 November 2007

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spinqualitylabelsall models 1kr7, resolution 1.5Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of the nerve tissue mini-hemoglobin from the nemertean worm Cerebratulus lacteus

Overview

A very short hemoglobin (CerHb; 109 amino acids) binds O(2) cooperatively, in the nerve tissue of the nemertean worm Cerebratulus lacteus to sustain, neural activity during anoxia. Sequence analysis suggests that CerHb, tertiary structure may be unique among the known globin fold evolutionary, variants. The X-ray structure of oxygenated CerHb (R factor 15.3%, at 1.5, A resolution) displays deletion of the globin N-terminal A helix, an, extended GH region, a very short H helix, and heme solvent shielding based, on specific aromatic residues. The heme-bound O(2) is stabilized by, hydrogen bonds to the distal TyrB10-GlnE7 pair. Ligand access to heme may, take place through a wide protein matrix tunnel connecting the distal site, to a surface cleft located between the E and H helices.

About this Structure

1KR7 is a Single protein structure of sequence from Cerebratulus lacteus with SO4, ACT, HEM and OXY as ligands. Full crystallographic information is available from OCA.

Reference

The 109 residue nerve tissue minihemoglobin from Cerebratulus lacteus highlights striking structural plasticity of the alpha-helical globin fold., Pesce A, Nardini M, Dewilde S, Geuens E, Yamauchi K, Ascenzi P, Riggs AF, Moens L, Bolognesi M, Structure. 2002 May;10(5):725-35. PMID:12015154

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