3lhb
From Proteopedia
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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
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