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  Quaternary structure of the European spiny lobster (Palinurus elephas) 1 x 6-mer hemocyanin from cryoEM and amino acid sequence data

Meissner, U., Stohr, M., Kusche, K., Burmester, T., Stark, H., Harris, J. R., et al. (2003). Quaternary structure of the European spiny lobster (Palinurus elephas) 1 x 6-mer hemocyanin from cryoEM and amino acid sequence data. Journal of Molecular Biology, 325(1), 99-109. Retrieved from http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6WK7-47C3H5G-G-1&_cdi=6899&_user=38661&_pii=S0022283602011737&_orig=search&_coverDate=01%2F03%2F2003&_sk=996749998&view=c&wchp=dGLbVlb-zSkzV&md5=ad700c4e35e9dd2bb5b05b9ae3469524&ie=/sdarticle.pdf.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-9421-4 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-39C2-D
Genre: Journal Article

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 Creators:
Meissner, U., Author
Stohr, M., Author
Kusche, K., Author
Burmester, T., Author
Stark, H.1, Author              
Harris, J. R., Author
Orlova, E. V., Author
Markl, J., Author
Affiliations:
1Research Group of 3D Electron Cryo-Microscopy, MPI for biophysical chemistry, Max Planck Society, ou_578577              

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Free keywords: 3D-EM; cryoelectron microscopy (cryoEM); 3D reconstruction; Crustacea; hemocyanin; quaternary structure
 Abstract: Arthropod hemocyanins are large respiratory proteins that are composed of up to 48 subunits (8 x 6-mer) in the 75 kDa range. A 3D reconstruction of the 1 x 6-mer hemocyanin from the European spiny lobster Palinuris elephas has been performed from 9970 single particles using cryoelectron microscopy. An 8 Angstrom 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. (C) 2002 Elsevier Science Ltd. All rights reserved

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Language(s): eng - English
 Dates: 2003-01-03
 Publication Status: Published in print
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 Rev. Method: Peer
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Title: Journal of Molecular Biology
Source Genre: Journal
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Pages: - Volume / Issue: 325 (1) Sequence Number: - Start / End Page: 99 - 109 Identifier: -