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1uij

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

Structural highlights

1uij is a 6 chain structure with sequence from Glycine max. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.5Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GLCB1_SOYBN Seed storage protein. Accumulates during seed development and is hydrolyzed after germination to provide a carbon and nitrogen source for the developing seedling.^[1]

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^[2]

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

References

↑ Harada JJ, Barker SJ, Goldberg RB. Soybean beta-conglycinin genes are clustered in several DNA regions and are regulated by transcriptional and posttranscriptional processes. Plant Cell. 1989 Apr;1(4):415-25. PMID:2562562 doi:10.1105/tpc.1.4.415
↑ 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 3: / Line 3: @@
 <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 [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1UIJ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1uij]] is a 6 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1UIJ FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1uik|1uik]]</div></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1uij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uij OCA], [https://pdbe.org/1uij PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uij RCSB], [https://www.ebi.ac.uk/pdbsum/1uij PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uij ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/GLCB_SOYBN 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.
+[https://www.uniprot.org/uniprot/GLCB1_SOYBN GLCB1_SOYBN] Seed storage protein. Accumulates during seed development and is hydrolyzed after germination to provide a carbon and nitrogen source for the developing seedling.<ref>PMID:2562562</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Glycine hispida]]
+[[Category: Glycine max]]
 [[Category: Large Structures]]
-[[Category: Maruyama, N]]
+[[Category: Maruyama N]]
-[[Category: Maruyama, Y]]
+[[Category: Maruyama Y]]
-[[Category: Okuda, E]]
+[[Category: Okuda E]]
-[[Category: Tsuruki, T]]
+[[Category: Tsuruki T]]
-[[Category: Utsumi, S]]
+[[Category: Utsumi S]]
-[[Category: Yoshikawa, M]]
+[[Category: Yoshikawa M]]
-[[Category: Double-stranded beta helix]]
-[[Category: Seed storage protein]]
-[[Category: Sugar binding protein]]

1uij

From Proteopedia

Current revision

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?)

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