Novel subunit structure observed for noncooperative hemoglobin from Urechis caupo

Prasanna Kolatkar, W. E. Meador, R. L. Stanfield, M. L. Hackert

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Abstract

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-Å resolution crystal structure reveals that although the individual subunits are β-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).

Original languageEnglish
Pages (from-to)3462-3465
Number of pages4
JournalJournal of Biological Chemistry
Volume263
Issue number7
Publication statusPublished - 1 Jan 1988
Externally publishedYes

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ASJC Scopus subject areas

  • Biochemistry

Cite this

Kolatkar, P., Meador, W. E., Stanfield, R. L., & Hackert, M. L. (1988). Novel subunit structure observed for noncooperative hemoglobin from Urechis caupo. Journal of Biological Chemistry, 263(7), 3462-3465.