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1uij

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Revision as of 00:25, 12 September 2015

Crystal Structure Of Soybean beta-Conglycinin Beta Homotrimer (I122M/K124W)

Structural highlights

1uij is a 6 chain structure with sequence from Glycine hispida. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1uik
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[GLCB_SOYBN] Seed storage protein. Accumulates during seed development and is hydrolyzed after germination to provide a carbon and nitrogen source for the developing seedling.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Maruyama N, Maruyama Y, Tsuruki T, Okuda E, Yoshikawa M, Utsumi S. Creation of soybean beta-conglycinin beta with strong phagocytosis-stimulating activity. Biochim Biophys Acta. 2003 May 30;1648(1-2):99-104. PMID:12758152

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1uij"

@@ Line 2: / Line 2: @@
 <StructureSection load='1uij' size='340' side='right' caption='[[1uij]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1uij]] is a 6 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UIJ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1uij]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Glycine_hispida Glycine hispida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UIJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UIJ FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1uik|1uik]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1uij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uij OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1uij RCSB], [http://www.ebi.ac.uk/pdbsum/1uij PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1uij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uij OCA], [http://pdbe.org/1uij PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1uij RCSB], [http://www.ebi.ac.uk/pdbsum/1uij PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 26: / Line 26: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1uij" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Glycine max]]
+[[Category: Glycine hispida]]
 [[Category: Maruyama, N]]
 [[Category: Maruyama, Y]]

1uij

From Proteopedia

Revision as of 00:25, 12 September 2015

Crystal Structure Of Soybean beta-Conglycinin Beta Homotrimer (I122M/K124W)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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