Nautilus pompilius Hemocyanin: 9 Å Cryo-EM Structure and Molecular Model Reveal the Subunit Pathway and the Interfaces between the 70 Functional Units

Autor: Frank Depoix, Ulrich Meissner, Arne Moeller, Jürgen Markl, Christos Gatsogiannis

Publikováno v: Gatsogiannis, C, Möller, A, Depoix, F, Meissner, U & Markl, J 2007, ' Nautilus pompilius hemocyanin : 9 A cryo-EM structure and molecular model reveal the subunit pathway and the interfaces between the 70 functional units ', Journal of Molecular Biology, vol. 374, no. 2, pp. 465-86 . https://doi.org/10.1016/j.jmb.2007.09.036

Hemocyanins are giant extracellular oxygen carriers in the hemolymph of many molluscs. Nautilus pompilius (Cephalopoda) hemocyanin is a cylindrical decamer of a 350 kDa polypeptide subunit that in turn is a "pearl-chain" of seven different functional

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::932357e9e148af65c03f1c0a9debb045
https://doi.org/10.1016/j.jmb.2007.09.036

Limulus polyphemus Hemocyanin: 10 Å Cryo-EM Structure, Sequence Analysis, Molecular Modelling and Rigid-body Fitting Reveal the Interfaces Between the Eight Hexamers

Autor: Jürgen Markl, Michael Stohr, Ulrich Meissner, Thorsten Burmester, Willy Wriggers, Kada Hammouti, Jochen Heyd, Silke Hagner-Holler, Frank Depoix, Andreas G. Martin

Publikováno v: Journal of Molecular Biology. 366:1332-1350

The blue copper protein hemocyanin from the horseshoe crab Limulus polyphemus is among the largest respiratory proteins found in nature (3.5 MDa) and exhibits a highly cooperative oxygen binding. Its 48 subunits are arranged as eight hexamers (1×6me

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4be3741b8c299e8974e26df533171c12
https://doi.org/10.1016/j.jmb.2006.11.075

Comparison of the decameric structure of peroxiredoxin-II by transmission electron microscopy and X-ray crystallography

Autor: Michail N. Isupov, J. Robin Harris, Alexei A. Vagin, Ulrich Meissner, Dirk Scheffler, Jennifer A. Littlechild, Ewald Schröder, Poul Kristensen

Publikováno v: Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1547:221-234

The decameric human erythrocyte protein torin is identical to the thiol-specific antioxidant protein-II (TSA-II), also termed peroxiredoxin-II (Prx-II). Single particle analysis from electron micrographs of Prx-II molecules homogeneously orientated a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::374ae8a148fa404137963165925600de
https://doi.org/10.1016/s0167-4838(01)00184-4

A new automated plunger for cryopreparation of proteins in defined - even oxygen free - atmospheres

Autor: Ulrich Meissner, Jürgen Markl, Frank Depoix

Publikováno v: EMC 2008 14th European Microscopy Congress 1–5 September 2008, Aachen, Germany ISBN: 9783540851547

We study the structure and function of hemocyanins. They are giant extracellular oxygen carriers in the hemolymph of many molluscs and arthropods. Since some of these blue, copper-containing proteins show the highest cooperativity in nature (h = 10),

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::2a29c50d60a6eb331a06dd8f64be90b4
https://doi.org/10.1007/978-3-540-85156-1_403

Allosterism of Nautilus pompilius hemocyanin as deduced from 8 Å cryo-EM structures obtained under oxy and deoxy conditions

Autor: Christos Gatsogiannis, Ulrich Meissner, Frank Depoix, Jürgen Markl, Arne Moeller

Publikováno v: EMC 2008 14th European Microscopy Congress 1–5 September 2008, Aachen, Germany ISBN: 9783540852278

Hemocyanins are the blue copper-containing respiratory proteins of many molluscs. Nautilus pompilius hemocyanin (NpH) is a cylindrical decamer composed of ten copies of a 350 kDa polypeptide subunit, in turn consisting of seven O2-binding functional

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::cd2bb2b239f2e026f91ede8deb526ee5
https://doi.org/10.1007/978-3-540-85228-5_20