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Two-dimensional cry...
Two-dimensional crystallization and electron crystallography of MAPEG proteins.
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- Hebert, Hans (author)
- Karolinska Institutet,Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH,Biovetenskaper och Nutrition, Karolinska Institutet
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- Jegerschöld, Caroline (author)
- Karolinska Institutet
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- Bhakat, Priyaranjan (author)
- Biovetenskaper och Nutrition, Karolinska Institutet
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- Holm, Peter J (author)
- Biovetenskaper och Nutrition, Karolinska Institutet
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Packer, L (author)
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(creator_code:org_t)
- 2005
- 2005
- English.
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In: Methods in Enzymology. - 0076-6879 .- 1557-7988. ; 401, s. 161-8
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Abstract
Subject headings
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- Members of the membrane-associated proteins in the eicosanoid and glutathione metabolism (MAPEG) superfamily have been subjected to two-dimensional crystallization experiments. A common denominator for successful attempts has been the use of a low lipid/protein ratio in the range of 1-9 (mol/mol). Electron crystallography demonstrated either hexagonal or orthorhombic packing of trimeric protein units. Three-dimensional structure analysis of the MAPEG member microsomal glutathione transferase 1 has shown that the monomer for this protein contains a left-handed bundle of four transmembrane helices. It is likely that this is a common structural motif for MAPEG proteins, because projection maps of all structurally characterized members are very similar.
Subject headings
- NATURVETENSKAP -- Biologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences (hsv//eng)
Publication and Content Type
- ref (subject category)
- art (subject category)
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