1phs
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1phs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1phs OCA], [http://www.ebi.ac.uk/pdbsum/1phs PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1phs RCSB]</span> | ||
}} | }} | ||
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[[Category: plant seed storage protein (vicilin)]] | [[Category: plant seed storage protein (vicilin)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:59:51 2008'' |
Revision as of 19:59, 30 March 2008
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| , resolution 3.0Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE THREE-DIMENSIONAL STRUCTURE OF THE SEED STORAGE PROTEIN PHASEOLIN AT 3 ANGSTROMS RESOLUTION
Overview
The polypeptides of the trimeric seed storage protein phaseolin comprise two structurally similar units each made up of a beta-barrel and an alpha-helical domain. The beta-barrel has the 'jelly-roll' folding topology of the viral coat proteins and the alpha-helical domain shows structural similarity to the helix-turn-helix motif found in certain DNA-binding proteins.
About this Structure
1PHS is a Single protein structure of sequence from Phaseolus vulgaris. Full crystallographic information is available from OCA.
Reference
The three-dimensional structure of the seed storage protein phaseolin at 3 A resolution., Lawrence MC, Suzuki E, Varghese JN, Davis PC, Van Donkelaar A, Tulloch PA, Colman PM, EMBO J. 1990 Jan;9(1):9-15. PMID:2295315
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