0000000000005949

AUTHOR

Michael Stohr

showing 4 related works from this author

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

2007

Abstract 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 (1×6mers) that form the native 8×6mer in a nested hierarchy of 2×6mers and 4×6mers. This quaternary structure is established by eight subunit types (termed I, IIA, II, IIIA, IIIB, IV, V, and VI), of which only type II has been sequenced. Crystal structures of the 1×6mer are available, but for the 8×6mer only a 40 A 3D reconstruction exists. Consequently, the structural parameters of the 8×6mer are not firmly established, and the molecular inte…

Models MolecularMolecular modelCryo-electron microscopyCopper proteinProtein subunitmedicine.medical_treatmentMolecular Sequence DataStructure-Activity RelationshipStructural BiologyHorseshoe CrabsmedicineAnimalsAmino Acid SequenceProtein Structure QuaternaryMolecular BiologyPhylogenySequence Homology Amino AcidbiologyCryoelectron MicroscopyHemocyaninbiology.organism_classificationProtein Structure TertiaryCrystallographyLimulusHemocyaninsProtein quaternary structureOxygen bindingJournal of Molecular Biology
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3-D reconstruction of hemocyanins and other invertebrate hemolymph proteins by cryo-TEM: an overview.

2004

Cryoelectron MicroscopyGeneral Physics and AstronomyCell BiologyAnatomyBiologyCryo temBiochemistryStructural BiologyHemolymphHemolymphHemocyaninsAnimalsGeneral Materials ScienceInvertebrateMicron (Oxford, England : 1993)
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Quaternary structure of the European spiny lobster (Palinurus elephas) 1x6-mer hemocyanin from cryoEM and amino acid sequence data.

2002

Abstract 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 A resolution of the hemocyanin 3D reconstruction has been obtained from about 600 final class averages. Visualisation of structural elements such as α-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…

Models MolecularPanulirusmedicine.medical_treatmentPalinurus elephasMolecular Sequence DataStatic ElectricityCrystallography X-RaySpecies SpecificityStructural BiologymedicineAnimalsAmino Acid SequencePalinuridaeProtein Structure QuaternaryMolecular BiologyPeptide sequencebiologySequence Homology Amino AcidResolution (electron density)Cryoelectron MicroscopyHemocyaninbiology.organism_classificationCrystallographyProtein SubunitsBiochemistryHemocyaninsProtein quaternary structureArthropodSpiny lobsterSequence AlignmentJournal of molecular biology
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Quaternary structure and molecular model of a 4x6mer arthropod hemocyanin in oxygenated and deoxygenated states by 3D cryo-electron microscopy

2007

Extended abstract of a paper presented at MC 2007, 33rd DGE Conference in Saarbrücken, Germany, September 2 – September 7, 2007

CrystallographyMolecular modelbiologyChemistryCryo-electron microscopymedicine.medical_treatmentBiophysicsmedicineProtein quaternary structureHemocyaninArthropodbiology.organism_classificationInstrumentationMicroscopy and Microanalysis
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