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Erythrocruorin

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Globin, extracellular
Lumbricus Erythrocruorin at 3.5A resolution.png
Lumbricus Erythrocruorin (PDB: 2GTL​)
Identifiers
SymbolHaemoglobin_extracell
InterProIPR014610
Annelid erythrocruorin linker subunit, C-terminal
Identifiers
SymbolEryth_link_C
PfamPF16915
InterProIPR031639
CATH2gtlM02
SCOP28029676 / SCOPe / SUPFAM
CDDcd11673

Erythrocruorin (from Greek eruthros "red" + Latin cruor "blood") is a large oxygen-carrying protein complex, which has a molecular mass greater than 3.5 million Daltons.[1] It is related to the similar chlorocruorin, both of which are sometimes dubbed giant hemoglobin and hexagonal bilayer haemoglobin. It is found in many annelids and arthropods (including some insects).[2]

Structure

Two structures of erythrocruorin have been resolved. The protein is a highly symmetric assembly made from heme-binding globins and unique linker proteins.[1][3]

References

  1. ^ a b Royer WE, Strand K, van Heel M, Hendrickson WA (June 2000). "Structural hierarchy in erythrocruorin, the giant respiratory assemblage of annelids". Proceedings of the National Academy of Sciences of the United States of America. 97 (13): 7107–11. doi:10.1073/pnas.97.13.7107. PMC 16507. PMID 10860978.
  2. ^ Ruggiero Bachega JF, Vasconcelos Maluf F, Andi B, D'Muniz Pereira H, Falsarella Carazzollea M, Orville AM, et al. (June 2015). "The structure of the giant haemoglobin from Glossoscolex paulistus". Acta Crystallographica. Section D, Biological Crystallography. 71 (Pt 6): 1257–71. doi:10.1107/S1399004715005453. PMID 26057666.
  3. ^ Pallavicini A, Negrisolo E, Barbato R, Dewilde S, Ghiretti-Magaldi A, Moens L, Lanfranchi G (July 2001). "The primary structure of globin and linker chains from the chlorocruorin of the polychaete Sabella spallanzanii". The Journal of Biological Chemistry. 276 (28): 26384–90. doi:10.1074/jbc.M006939200. PMID 11294828.

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