2gtl
From Proteopedia
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Lumbricus Erythrocruorin at 3.5A resolution
Overview
Annelid erythrocruorins are highly cooperative extracellular respiratory, proteins with molecular masses on the order of 3.6 million Daltons. We, report here the 3.5 A crystal structure of erythrocruorin from the, earthworm Lumbricus terrestris. This structure reveals details of, symmetrical and quasi-symmetrical interactions that dictate the, self-limited assembly of 144 hemoglobin and 36 linker subunits. The linker, subunits assemble into a core complex with D(6) symmetry onto which 12, hemoglobin dodecamers bind to form the entire complex. Although the three, unique linker subunits share structural similarity, their interactions, with each other and the hemoglobin subunits display striking diversity., The observed diversity includes design features that have been, incorporated into the linker subunits and may be critical for efficient, assembly of large quantities of this complex respiratory protein.
About this Structure
2GTL is a Protein complex structure of sequences from Lumbricus terrestris with CA, ZN, CMO and HEM as ligands. Full crystallographic information is available from OCA.
Reference
Lumbricus erythrocruorin at 3.5 A resolution: architecture of a megadalton respiratory complex., Royer WE Jr, Sharma H, Strand K, Knapp JE, Bhyravbhatla B, Structure. 2006 Jul;14(7):1167-77. PMID:16843898
Page seeded by OCA on Thu Nov 8 13:30:57 2007
