Structural analysis of Urechis caupo hemoglobin

Prasanna Kolatkar, Marvin L. Hackert, Austen F. Riggs

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

The structure of Urechis caupo hemoglobin in the cyanomet state has been refined to R = 0.148 at 2.5 A resolution. Although the tertiary structure is similar to that of other vertebrate and invertebrate hemoglobins the quaternary structures of this tetramer is unique as suggested by the earlier determination of the 5.0 Å resolution structure. The G and H helices of the hemoglobin are on the outside of the tetramer facing the solvent in contrast to human hemoglobin where the G and H helices form inter-subunit contacts. A substantial number of tightly bound water molecules help mediate interactions between subunits. The unusual arrangement of subunits is consistent with the general lack of cooperativity of oxygen uptake for Urechis caupo hemoglobin.

Original languageEnglish
Pages (from-to)87-97
Number of pages11
JournalJournal of Molecular Biology
Volume237
Issue number1
DOIs
Publication statusPublished - 18 May 1994
Externally publishedYes

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Hemoglobin H
Invertebrates
Vertebrates
Hemoglobins
Oxygen
Water
Urechis caupo hemoglobin

Keywords

  • invertebrate hemoglobin
  • quaternary structure
  • X-ray structure

ASJC Scopus subject areas

  • Virology

Cite this

Structural analysis of Urechis caupo hemoglobin. / Kolatkar, Prasanna; Hackert, Marvin L.; Riggs, Austen F.

In: Journal of Molecular Biology, Vol. 237, No. 1, 18.05.1994, p. 87-97.

Research output: Contribution to journalArticle

Kolatkar, Prasanna ; Hackert, Marvin L. ; Riggs, Austen F. / Structural analysis of Urechis caupo hemoglobin. In: Journal of Molecular Biology. 1994 ; Vol. 237, No. 1. pp. 87-97.
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