Novel subunit structure observed for noncooperative hemoglobin from Urechis caupo

Tetrameric hemoglobin from the “fat innkeeper” worm Urechis caupo possesses a novel subunit arrangement having an “inside out” quaternary structure in that the G/H helices are located on the outer surface of the tetramer. A 5-A resolution crystal structure reveals that although the individual subuni...

Full description

Saved in:
Bibliographic Details
Published in:The Journal of biological chemistry 1988-03, Vol.263 (7), p.3462-3465
Main Authors: Kolatkar, P R, Meador, W E, Stanfield, R L, Hackert, M L
Format: Article
Language:English
Subjects:
Animals
biochemistry
Biological and medical sciences
Crystallography
Disulfides
Fundamental and applied biological sciences. Psychology
hemoglobin
Hemoglobins
Humans
Invertebrates - analysis
Macromolecular Substances
Marine
Molecular biophysics
molecular structure
Protein Conformation
Structure in molecular biology
Tridimensional structure
Urechis caupo
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Tetrameric hemoglobin from the “fat innkeeper” worm Urechis caupo possesses a novel subunit arrangement having an “inside out” quaternary structure in that the G/H helices are located on the outer surface of the tetramer. A 5-A resolution crystal structure reveals that although the individual subunits are beta-like, having a distinct D helix and the general myoglobin fold, the subunit contacts are very different from those previously observed for hemoglobins. Furthermore, the hemoglobin from U. caupo is also quite different from the unusual hemoglobin tetramer from clam which also has its G/H helices on the outer surface but with the hemes in close proximity through E-F helical contacts (Royer, W. E., Jr., Love, W. E., and Fenderson, F. F. (1985) Nature 316, 277-280).
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)69093-3