1uij
From Proteopedia
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| - | [[Image:1uij.gif|left|200px]] | + | [[Image:1uij.gif|left|200px]] |
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| - | '''Crystal Structure Of Soybean beta-Conglycinin Beta Homotrimer (I122M/K124W)''' | + | {{Structure |
| + | |PDB= 1uij |SIZE=350|CAPTION= <scene name='initialview01'>1uij</scene>, resolution 2.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Crystal Structure Of Soybean beta-Conglycinin Beta Homotrimer (I122M/K124W)''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1UIJ is a [ | + | 1UIJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UIJ OCA]. |
==Reference== | ==Reference== | ||
| - | Creation of soybean beta-conglycinin beta with strong phagocytosis-stimulating activity., Maruyama N, Maruyama Y, Tsuruki T, Okuda E, Yoshikawa M, Utsumi S, Biochim Biophys Acta. 2003 May 30;1648(1-2):99-104. PMID:[http:// | + | Creation of soybean beta-conglycinin beta with strong phagocytosis-stimulating activity., Maruyama N, Maruyama Y, Tsuruki T, Okuda E, Yoshikawa M, Utsumi S, Biochim Biophys Acta. 2003 May 30;1648(1-2):99-104. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12758152 12758152] |
[[Category: Glycine max]] | [[Category: Glycine max]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: seed storage protein]] | [[Category: seed storage protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:32:30 2008'' |
Revision as of 12:32, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure Of Soybean beta-Conglycinin Beta Homotrimer (I122M/K124W)
Overview
beta-Conglycinin is composed of three kinds of subunit: alpha, alpha' and beta. A phagocytosis-stimulating peptide sequence (MITLAIPVNKPGR), soymetide, exists in the alpha' subunit of beta-conglycinin. Met at N terminus of the soymetide is essential for the activity. When Thr at the third residue from N terminus of the soymetide is replaced by Phe or Trp, the phagocytosis-stimulating activity greatly increases (Thr<Phe<Trp). The beta subunit does not exhibit the phagocytosis-stimulating activity because the residues corresponding to the first and third residues in the soymetide are Ile and Lys, respectively. In this study, we introduced the phagocytosis-stimulating peptide sequence (Ile-->Met, Lys-->Thr, Phe, or Trp) into the beta subunit after confirmation of the effects of residue replacements by molecular modeling, suggesting that the introduced mutations might not prevent the correct folding. The studies of circular dichroism (CD), gel filtration and differential scanning calorimetry (DSC) of the mutants (I122M/K124T, I122M/K124F, I122M/K124W) expressed in E. coli demonstrated that they folded and self-assembled similarly to the wild type. This was confirmed by X-ray analysis of I122M/K124W crystal where the biggest residue tryptophane was introduced. The three mutants exhibited phagocytosis activities after digestion by trypsin, and the order was the wild type<I122M/K124T<I122M/K124F<I122M/K124W as expected.
About this Structure
1UIJ is a Single protein structure of sequence from Glycine max. Full crystallographic information is available from OCA.
Reference
Creation of soybean beta-conglycinin beta with strong phagocytosis-stimulating activity., Maruyama N, Maruyama Y, Tsuruki T, Okuda E, Yoshikawa M, Utsumi S, Biochim Biophys Acta. 2003 May 30;1648(1-2):99-104. PMID:12758152
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