2GTL

Lumbricus Erythrocruorin at 3.5A resolution

Summary for 2GTL

• Entry DOI: 10.2210/pdb2gtl/pdb
• Descriptor: Extracellular globin 4, CALCIUM ION, ZINC ION, ... (11 entities in total)
• Functional Keywords: annelid erythrocruorins, respiratory protein, hexagonal bilayer, dihedral d6 symmetry, triple stranded helical coils, oxygen storage-transport complex, oxygen storage/transport
• Biological source: Lumbricus terrestris (common earthworm); More
• Cellular location: Secreted: P13579 P11069
• Total number of polymer chains: 15
• Total formula weight: 283905.29

Authors

Royer Jr., W.E.,Sharma, H.,Strand, K.,Knapp, J.E.,Bhyravbhatla, B. (deposition date: 2006-04-28, release date: 2006-07-18, Last modification date: 2024-10-30)

Primary citation

Royer Jr., W.E.,Sharma, H.,Strand, K.,Knapp, J.E.,Bhyravbhatla, B.
Lumbricus erythrocruorin at 3.5 a resolution: architecture of a megadalton respiratory complex.
Structure, 14:1167-1177, 2006

PubMed Abstract: 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.

PubMed: 16843898
DOI: 10.1016/j.str.2006.05.011

Experimental method

X-RAY DIFFRACTION (3.5 Å)