1ucx
From Proteopedia
(New page: 200px<br /><applet load="1ucx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ucx, resolution 3.2Å" /> '''Crystal structure of ...) |
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| - | [[Image:1ucx.gif|left|200px]]<br /><applet load="1ucx" size=" | + | [[Image:1ucx.gif|left|200px]]<br /><applet load="1ucx" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ucx, resolution 3.2Å" /> | caption="1ucx, resolution 3.2Å" /> | ||
'''Crystal structure of proglycinin C12G mutant'''<br /> | '''Crystal structure of proglycinin C12G mutant'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The constituent subunits of seed storage protein 11S globulin have two | + | The constituent subunits of seed storage protein 11S globulin have two disulfide bonds that are common among 11S globulins from legume and nonlegume seeds. In the case of the A1aB1b subunit of soybean 11S globulin, glycinin, Cys12-Cys45 and Cys88-Cys298 are observed by X-ray crystallography. The significance of these two disulfide bonds for structural stability was investigated by mutagenesis of Cys12 to Gly and of Cys88 to Ser. The disulfide bond-deficient mutants C12G and C88S could form the correct conformations identical to that of the wild-type proglycinin except in the vicinities of the mutation sites C12 and C88 as shown by their crystal structures. Thermal stability monitored by differential scanning calorimetry of the mutants indicated that the contribution of these disulfide bonds to the thermal stability of proglycinin A1aB1b is low, although there is a small difference in the extent of the contribution between the two disulfide bonds (Cys12-Cys45 > Cys88-Cys298). The contribution of Cys88-Cys298 to the resistance of proglycinin A1aB1b to proteinase digestion is higher than that of Cys12-Cys45. Possible effects of structure on the different properties of C12G and C88S are discussed. |
==About this Structure== | ==About this Structure== | ||
| - | 1UCX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http:// | + | 1UCX is a [http://en.wikipedia.org/wiki/Single_protein 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=1UCX OCA]. |
==Reference== | ==Reference== | ||
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[[Category: trimer]] | [[Category: trimer]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:23:06 2008'' |
Revision as of 13:23, 21 February 2008
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Crystal structure of proglycinin C12G mutant
Overview
The constituent subunits of seed storage protein 11S globulin have two disulfide bonds that are common among 11S globulins from legume and nonlegume seeds. In the case of the A1aB1b subunit of soybean 11S globulin, glycinin, Cys12-Cys45 and Cys88-Cys298 are observed by X-ray crystallography. The significance of these two disulfide bonds for structural stability was investigated by mutagenesis of Cys12 to Gly and of Cys88 to Ser. The disulfide bond-deficient mutants C12G and C88S could form the correct conformations identical to that of the wild-type proglycinin except in the vicinities of the mutation sites C12 and C88 as shown by their crystal structures. Thermal stability monitored by differential scanning calorimetry of the mutants indicated that the contribution of these disulfide bonds to the thermal stability of proglycinin A1aB1b is low, although there is a small difference in the extent of the contribution between the two disulfide bonds (Cys12-Cys45 > Cys88-Cys298). The contribution of Cys88-Cys298 to the resistance of proglycinin A1aB1b to proteinase digestion is higher than that of Cys12-Cys45. Possible effects of structure on the different properties of C12G and C88S are discussed.
About this Structure
1UCX is a Single protein structure of sequence from Glycine max. Full crystallographic information is available from OCA.
Reference
Crystal structures and structural stabilities of the disulfide bond-deficient soybean proglycinin mutants C12G and C88S., Adachi M, Okuda E, Kaneda Y, Hashimoto A, Shutov AD, Becker C, Muntz K, Utsumi S, J Agric Food Chem. 2003 Jul 30;51(16):4633-9. PMID:14705889
Page seeded by OCA on Thu Feb 21 15:23:06 2008
Categories: Glycine max | Single protein | Adachi, M. | Utsumi, S. | Mutant | Proglycinin | Soybean | Trimer
