This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
3lhb
From Proteopedia
|
THE 2.7 ANGSTROM CRYSTAL STRUCTURE OF DEOXYGENATED HEMOGLOBIN FROM THE SEA LAMPREY (PETROMYZON MARINUS)
Overview
BACKGROUND: The hemoglobins of the sea lamprey are unusual in that, cooperativity and sensitivity to pH arise from an equilibrium between a, high-affinity monomer and a low-affinity oligomer. Although the crystal, structure of the monomeric cyanide derivative has previously been, determined, the manner by which oligomerization acts to lower the oxygen, affinity and confer a strong Bohr effect has, until now, been speculative., RESULTS: We have determined the crystal structure of deoxygenated lamprey, hemoglobin V by molecular replacement to 2.7 A resolution, in a crystal, form with twelve protomers in the asymmetric unit. The subunits are, arranged as six essentially identical dimers, with a novel subunit, interface formed by the E helices and the AB corner using the standard, hemoglobin ... [(full description)]
About this Structure
3LHB is a [Single protein] structure of sequence from [Petromyzon marinus] with HEM as [ligand]. Structure known Active Sites: F10, F11, F12, FE1, FE2, FE3, FE4, FE5, FE6, FE7, FE8 and FE9. Full crystallographic information is available from [OCA].
Reference
The 2.7 A crystal structure of deoxygenated hemoglobin from the sea lamprey (Petromyzon marinus): structural basis for a lowered oxygen affinity and Bohr effect., Heaslet HA, Royer WE Jr, Structure. 1999 May;7(5):517-26. PMID:10378271
Page seeded by OCA on Tue Oct 30 17:45:37 2007
