The three-dimensional structure of the seed storage protein phaseolin at 3 A resolution
- PMID: 2295315
- PMCID: PMC551622
- DOI: 10.1002/j.1460-2075.1990.tb08074.x
The three-dimensional structure of the seed storage protein phaseolin at 3 A resolution
Abstract
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.
Similar articles
-
A phaseolin domain involved directly in trimer assembly is a determinant for binding by the chaperone BiP.Plant Cell. 2003 Oct;15(10):2464-75. doi: 10.1105/tpc.013052. Epub 2003 Sep 24. Plant Cell. 2003. PMID: 14508011 Free PMC article.
-
Structure of phaseolin at 2.2 A resolution. Implications for a common vicilin/legumin structure and the genetic engineering of seed storage proteins.J Mol Biol. 1994 May 20;238(5):748-76. doi: 10.1006/jmbi.1994.1333. J Mol Biol. 1994. PMID: 8182747
-
The refined structure of canavalin from jack bean in two crystal forms at 2.1 and 2.0 A resolution.Acta Crystallogr D Biol Crystallogr. 2000 Apr;56(Pt 4):411-20. doi: 10.1107/s0907444900002237. Acta Crystallogr D Biol Crystallogr. 2000. PMID: 10739914
-
The structure of tumour necrosis factor--implications for biological function.J Cell Sci Suppl. 1990;13:11-8. doi: 10.1242/jcs.1990.supplement_13.3. J Cell Sci Suppl. 1990. PMID: 1964681
-
Folding, aggregation and molecular recognition in peptides.Acta Crystallogr B. 1992 Aug 1;48 ( Pt 4):341-56. doi: 10.1107/s0108768192000673. Acta Crystallogr B. 1992. PMID: 1418817 Review.
Cited by
-
Extensive modifications for methionine enhancement in the beta-barrels do not alter the structural stability of the bean seed storage protein phaseolin.J Protein Chem. 1995 Nov;14(8):665-78. doi: 10.1007/BF01886905. J Protein Chem. 1995. PMID: 8747427
-
Deposition of storage proteins.Plant Mol Biol. 1998 Sep;38(1-2):77-99. Plant Mol Biol. 1998. PMID: 9738961 Review.
-
Seed storage proteins: structures and biosynthesis.Plant Cell. 1995 Jul;7(7):945-56. doi: 10.1105/tpc.7.7.945. Plant Cell. 1995. PMID: 7640527 Free PMC article. Review. No abstract available.
-
Endosperm origin, development, and function.Plant Cell. 1993 Oct;5(10):1383-99. doi: 10.1105/tpc.5.10.1383. Plant Cell. 1993. PMID: 8281040 Free PMC article. Review. No abstract available.
-
A phaseolin domain involved directly in trimer assembly is a determinant for binding by the chaperone BiP.Plant Cell. 2003 Oct;15(10):2464-75. doi: 10.1105/tpc.013052. Epub 2003 Sep 24. Plant Cell. 2003. PMID: 14508011 Free PMC article.
References
MeSH terms
Substances
LinkOut - more resources
Full Text Sources