MersV1, France, Analysis, bibRecord, 000238

Lumbricus terrestris Hemoglobin—The Architecture of Linker Chains and Structural Variation of the Central Toroid

Identifieur interne : 000238 ( France/Analysis ); précédent : 000237; suivant : 000239

Lumbricus terrestris Hemoglobin—The Architecture of Linker Chains and Structural Variation of the Central Toroid

Auteurs : Fabrice Mouche [France] ; Nicolas Boisset [France] ; Pawel A. Penczek

Source :

Journal of Structural Biology [ 1047-8477 ] ; 2001.

RBID : ISTEX:ADA314D4F80F8C1A4470ECBE1793327BBA8C987B

English descriptors

Abstract

Abstract: The extracellular giant hemoglobin from the earthworm Lumbricus terrestris was reconstructed at 14.9-Å resolution from cryo-electron microscope images, using a new procedure for estimating parameters of the contrast transfer (CTF) function. In this approach, two important CTF parameters, defocus and amplitude contrast ratio, can be refined iteratively within the framework of 3D projection alignment procedure, using minimization of sign disagreement between theoretical CTF and cross-resolution curves. The 3D cryo-EM map is in overall good agreement with the recent X-ray crystallography map of Royer et al. (2000, Proc. Natl. Acad. Sci. USA 97, 7107–7111), and it reveals the local threefold arrangement of the three linker chains present within each 1/12 of the complex. The 144 globin chains and 36 linker chains within the complex are clearly visible, and the interdigitation of the 12 coiled-coil helical spokes forming the central toroidal piece is confirmed. Based on these findings, two mechanisms of the dodecameric unit assembly are proposed and termed “zigzag” and “pairwise” polymerizations. However, the detection by cryo-EM of 12 additional rod-like bodies within the toroid raises the possibility that the architecture of the toroid is more complex than previously thought or that yet unknown ligands or allosteric effectors for this oxygen carrier are present.

Url:

https://api.istex.fr/ark:/67375/6H6-3NJT49HX-T/fulltext.pdf

DOI: 10.1006/jsbi.2001.4362

Affiliations:

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Le document en format XML

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<author><name sortKey="Boisset, Nicolas" sort="Boisset, Nicolas" uniqKey="Boisset N" first="Nicolas" last="Boisset">Nicolas Boisset</name>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>contrast transfer function</term>
<term>cryo-electron microscopy</term>
<term>field emission gun</term>
<term>hemoglobin</term>
<term>three-dimensional reconstruction</term>
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<keywords scheme="Teeft" xml:lang="en"><term>Additional bodies</term>
<term>Additional pieces</term>
<term>Amplitude contrast</term>
<term>Amplitude contrast ratio</term>
<term>Biol</term>
<term>Biophys</term>
<term>Black dots</term>
<term>Black triangle</term>
<term>Boisset</term>
<term>Central toroid</term>
<term>Central toroid piece</term>
<term>Central toroidal piece</term>
<term>Chains</term>
<term>Chem</term>
<term>Comparative study</term>
<term>Connector</term>
<term>Contrast transfer</term>
<term>Contrast transfer function</term>
<term>Crossresolution curve</term>
<term>Curved peduncle</term>
<term>Curved peduncles</term>
<term>Defocus</term>
<term>Defocus group</term>
<term>Defocus spread</term>
<term>Defocus values</term>
<term>Density maps</term>
<term>Dodecameric</term>
<term>Dodecameric hgss</term>
<term>Earthworm</term>
<term>Earthworm hemoglobin</term>
<term>Earthworm lumbricus terrestris</term>
<term>Electron microscope</term>
<term>Electron microscopy</term>
<term>Extracellular</term>
<term>Extracellular hemoglobin</term>
<term>Fourier</term>
<term>Fourier amplitudes</term>
<term>Fourier shell correlation</term>
<term>Fourier space</term>
<term>Globin</term>
<term>Globin chains</term>
<term>Helical</term>
<term>Helical spokes</term>
<term>Hemoglobin</term>
<term>Hexagonal</term>
<term>Hexagonal rings</term>
<term>Hexagonal structures</term>
<term>Hgss</term>
<term>Horizontal axis</term>
<term>Kuchumov</term>
<term>Lamy</term>
<term>Large plateau</term>
<term>Linker</term>
<term>Linker bodies</term>
<term>Linker body</term>
<term>Linker chain</term>
<term>Linker chains</term>
<term>Long arms</term>
<term>Lumbricus</term>
<term>Lumbricus hemoglobin</term>
<term>Lumbricus terrestris</term>
<term>Lumbricus terrestris hemoglobin</term>
<term>Macromolecule</term>
<term>Main branches</term>
<term>Micrograph</term>
<term>Micrographs</term>
<term>Molecular mass</term>
<term>Mouche</term>
<term>Offshoot</term>
<term>Open circles</term>
<term>Open dots</term>
<term>Orientation parameters</term>
<term>Pairwise</term>
<term>Peduncle</term>
<term>Penczek</term>
<term>Pillar</term>
<term>Pixel</term>
<term>Pixel size</term>
<term>Power spectrum</term>
<term>Projection alignment procedure</term>
<term>Quaternary structure</term>
<term>Riggs</term>
<term>Royer</term>
<term>Sinusoid</term>
<term>Sinusoid pillars</term>
<term>Sinusoidal pillars</term>
<term>Structural features</term>
<term>Substructure</term>
<term>Subunit</term>
<term>Superposed</term>
<term>Superposed dodecameric hgss</term>
<term>Surface representations</term>
<term>Taveau</term>
<term>Terrestris</term>
<term>Thon rings</term>
<term>Threefold symmetry</term>
<term>Toroid</term>
<term>Triangular coil</term>
<term>Triplet</term>
<term>Ultramicroscopy</term>
<term>Upper part</term>
<term>Vertical axis</term>
<term>Vinogradov</term>
<term>White arrow</term>
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<front><div type="abstract" xml:lang="en">Abstract: The extracellular giant hemoglobin from the earthworm Lumbricus terrestris was reconstructed at 14.9-Å resolution from cryo-electron microscope images, using a new procedure for estimating parameters of the contrast transfer (CTF) function. In this approach, two important CTF parameters, defocus and amplitude contrast ratio, can be refined iteratively within the framework of 3D projection alignment procedure, using minimization of sign disagreement between theoretical CTF and cross-resolution curves. The 3D cryo-EM map is in overall good agreement with the recent X-ray crystallography map of Royer et al. (2000, Proc. Natl. Acad. Sci. USA 97, 7107–7111), and it reveals the local threefold arrangement of the three linker chains present within each 1/12 of the complex. The 144 globin chains and 36 linker chains within the complex are clearly visible, and the interdigitation of the 12 coiled-coil helical spokes forming the central toroidal piece is confirmed. Based on these findings, two mechanisms of the dodecameric unit assembly are proposed and termed “zigzag” and “pairwise” polymerizations. However, the detection by cryo-EM of 12 additional rod-like bodies within the toroid raises the possibility that the architecture of the toroid is more complex than previously thought or that yet unknown ligands or allosteric effectors for this oxygen carrier are present.</div>
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Lumbricus terrestris Hemoglobin—The Architecture of Linker Chains and Structural Variation of the Central Toroid

Lumbricus terrestris Hemoglobin—The Architecture of Linker Chains and Structural Variation of the Central Toroid

Source :

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Links to Exploration step

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Pour manipuler ce document sous Unix (Dilib)

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