Comparative electron microscopy and image analysis of oxy- and deoxy-hemocyanin from the spiny lobster Panulirus interruptus

Haas, Felix de; Breemen, J.F.L. van; Boekema, Egbert J.; Keegstra, Wilko; Bruggen, E.F.J. Van

doi:10.1016/0304-3991(93)90248-v

Cited by 11 publications

(1 citation statement)

References 19 publications

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“…Assuming that the arrangement of the subunits within the hexamer changes during deoxygenation, as described by de Haas et al, 32 there is a high degree of similarity of the quaternary structure of our PelHc reconstruction with the X-ray data of PinHc 11 (obtained using oxygenated hemocyanin). This led us to the likely conclusion that we had prepared oxygenated hemocyanin.…”

Section: Conclusion and Future Perspectivesmentioning

confidence: 99%

Quaternary Structure of the European Spiny Lobster (Palinurus elephas) 1×6-mer Hemocyanin from cryoEM and Amino Acid Sequence Data

Meissner

Stöhr

Kusche

et al. 2003

Journal of Molecular Biology

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Arthropod hemocyanins are large respiratory proteins that are composed of up to 48 subunits (8 £ 6-mer) in the 75 kDa range. A 3D reconstruction of the 1 £ 6-mer hemocyanin from the European spiny lobster Palinurus elephas has been performed from 9970 single particles using cryoelectron microscopy. An 8 Å resolution of the hemocyanin 3D reconstruction has been obtained from about 600 final class averages. Visualisation of structural elements such as a-helices has been achieved. An amino acid sequence alignment shows the high sequence identity (. 80%) of the hemocyanin subunits from the European spiny lobster P. elephas and the American spiny lobster Panulirus interruptus. Comparison of the P. elephas hemocyanin electron microscopy (EM) density map with the known P. interruptus X-ray structure shows a close structural correlation, demonstrating the reliability of both methods for reconstructing proteins. By molecular modelling, we have found the putative locations for the amino acid sequence (597 -605) and the C-terminal end (654 -657), which are absent in the available P. interruptus X-ray data.

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Section: Conclusion and Future Perspectivesmentioning

confidence: 99%

Quaternary Structure of the European Spiny Lobster (Palinurus elephas) 1×6-mer Hemocyanin from cryoEM and Amino Acid Sequence Data

Meissner

Stöhr

Kusche

et al. 2003

Journal of Molecular Biology

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Hemocyanins from Arthropods and Molluscs

Magnus

2004

Handbook of Metalloproteins

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Copper Proteins with Dinuclear Active SitesBased in part on the article Copper Proteins with Dinuclear Active Sites by Konrad Lerch which appeared in theEncyclopedia of Inorganic Chemistry, First Edition.

Decker

2005

Encyclopedia of Inorganic Chemistry

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Copper proteins with dinuclear active sites comprise proteins with different structures and functions. The phenoloxidase, tyrosinase, and catecholoxidase are responsible for browning by starting the synthesis of melanin. These enzymes are involved in the primary immune response in invertebrates, plants, fungi as well as in the sclerotization of arthropods. The respiratory proteins hemocyanins are responsible for oxygen transport in some arthropods and molluscs. However, they can be converted to enzymes exhibiting phenoloxidase activity. Based on X‐ray structures of hemocyanins and a catecholoxidase, large parts of folding motifs are very similar although the sequence identities are far below 30%. A model for the activation process of phenoloxidase activity is presented.

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Comparative electron microscopy and image analysis of oxy- and deoxy-hemocyanin from the spiny lobster Panulirus interruptus

Cited by 11 publications

References 19 publications

Quaternary Structure of the European Spiny Lobster (Palinurus elephas) 1×6-mer Hemocyanin from cryoEM and Amino Acid Sequence Data

Quaternary Structure of the European Spiny Lobster (Palinurus elephas) 1×6-mer Hemocyanin from cryoEM and Amino Acid Sequence Data

Hemocyanins from Arthropods and Molluscs

Copper Proteins with Dinuclear Active SitesBased in part on the article Copper Proteins with Dinuclear Active Sites by Konrad Lerch which appeared in theEncyclopedia of Inorganic Chemistry, First Edition.

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