TY - JOUR
T1 - Novel subunit structure observed for noncooperative hemoglobin from Urechis caupo
AU - Kolatkar, P. R.
AU - Meador, W. E.
AU - Stanfield, R. L.
AU - Hackert, M. L.
PY - 1988
Y1 - 1988
N2 - 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).
AB - 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).
UR - http://www.scopus.com/inward/record.url?scp=0023869617&partnerID=8YFLogxK
M3 - Article
C2 - 3343252
AN - SCOPUS:0023869617
SN - 0021-9258
VL - 263
SP - 3462
EP - 3465
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 7
ER -