3xim
From Proteopedia
(New page: 200px<br /><applet load="3xim" size="450" color="white" frame="true" align="right" spinBox="true" caption="3xim, resolution 2.3Å" /> '''ARGININE RESIDUES AS ...) |
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| - | [[Image:3xim.jpg|left|200px]]<br /><applet load="3xim" size=" | + | [[Image:3xim.jpg|left|200px]]<br /><applet load="3xim" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="3xim, resolution 2.3Å" /> | caption="3xim, resolution 2.3Å" /> | ||
'''ARGININE RESIDUES AS STABILIZING ELEMENTS IN PROTEINS'''<br /> | '''ARGININE RESIDUES AS STABILIZING ELEMENTS IN PROTEINS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Site-specific substitutions of arginine for lysine in the thermostable | + | Site-specific substitutions of arginine for lysine in the thermostable D-xylose isomerase (XI) from Actinoplanes missouriensis are shown to impart significant heat stability enhancement in the presence of sugar substrates most probably by interfering with nonenzymatic glycation. The same substitutions are also found to increase heat stability in the absence of any sugar derivatives, where a mechanism based on prevention of glycation can no longer be invoked. This rather conservative substitution is moreover shown to improve thermostability in two other structurally unrelated proteins, human copper, zinc-superoxide dismutase (CuZnSOD) and D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from Bacillus subtilis. The stabilizing effect of Lys----Arg substitutions is rationalized on the basis of a detailed analysis of the crystal structures of wild-type XI and of engineered variants with Lys----Arg substitution at four distinct locations, residues 253, 309, 319, and 323. Molecular model building analysis of the structures of wild-type and mutant CuZnSOD (K9R) and GAPDH (G281K and G281R) is used to explain the observed stability enhancement in these proteins. In addition to demonstrating that even thermostable proteins can lend themselves to further stability improvement, our findings provide direct evidence that arginine residues are important stabilizing elements in proteins. Moreover, the stabilizing role of electrostatic interactions, particularly between subunits in oligomeric proteins, is documented. |
==About this Structure== | ==About this Structure== | ||
| - | 3XIM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Actinoplanes_missouriensis Actinoplanes missouriensis] with SOR and CO as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Xylose_isomerase Xylose isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.5 5.3.1.5] Full crystallographic information is available from [http:// | + | 3XIM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Actinoplanes_missouriensis Actinoplanes missouriensis] with <scene name='pdbligand=SOR:'>SOR</scene> and <scene name='pdbligand=CO:'>CO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Xylose_isomerase Xylose isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.5 5.3.1.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3XIM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Xylose isomerase]] | [[Category: Xylose isomerase]] | ||
| - | [[Category: Brande, I | + | [[Category: Brande, I Van Den.]] |
[[Category: Chiadmi, M.]] | [[Category: Chiadmi, M.]] | ||
[[Category: Demaeyer, M.]] | [[Category: Demaeyer, M.]] | ||
| - | [[Category: Denbroek, A | + | [[Category: Denbroek, A Van.]] |
[[Category: Janin, J.]] | [[Category: Janin, J.]] | ||
[[Category: Jenkins, J.]] | [[Category: Jenkins, J.]] | ||
| - | [[Category: Lambeir, A | + | [[Category: Lambeir, A M.]] |
[[Category: Laroche, Y.]] | [[Category: Laroche, Y.]] | ||
[[Category: Lasters, I.]] | [[Category: Lasters, I.]] | ||
[[Category: Matthyssens, G.]] | [[Category: Matthyssens, G.]] | ||
| - | [[Category: Mrabet, N | + | [[Category: Mrabet, N T.]] |
| - | [[Category: Quax, W | + | [[Category: Quax, W J.]] |
[[Category: Rey, F.]] | [[Category: Rey, F.]] | ||
[[Category: Stanssens, P.]] | [[Category: Stanssens, P.]] | ||
[[Category: Vantilbeurgh, H.]] | [[Category: Vantilbeurgh, H.]] | ||
| - | [[Category: Wodak, S | + | [[Category: Wodak, S J.]] |
[[Category: CO]] | [[Category: CO]] | ||
[[Category: SOR]] | [[Category: SOR]] | ||
[[Category: isomerase(intramolecular oxidoreductse)]] | [[Category: isomerase(intramolecular oxidoreductse)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:11:47 2008'' |
Revision as of 17:11, 21 February 2008
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ARGININE RESIDUES AS STABILIZING ELEMENTS IN PROTEINS
Overview
Site-specific substitutions of arginine for lysine in the thermostable D-xylose isomerase (XI) from Actinoplanes missouriensis are shown to impart significant heat stability enhancement in the presence of sugar substrates most probably by interfering with nonenzymatic glycation. The same substitutions are also found to increase heat stability in the absence of any sugar derivatives, where a mechanism based on prevention of glycation can no longer be invoked. This rather conservative substitution is moreover shown to improve thermostability in two other structurally unrelated proteins, human copper, zinc-superoxide dismutase (CuZnSOD) and D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from Bacillus subtilis. The stabilizing effect of Lys----Arg substitutions is rationalized on the basis of a detailed analysis of the crystal structures of wild-type XI and of engineered variants with Lys----Arg substitution at four distinct locations, residues 253, 309, 319, and 323. Molecular model building analysis of the structures of wild-type and mutant CuZnSOD (K9R) and GAPDH (G281K and G281R) is used to explain the observed stability enhancement in these proteins. In addition to demonstrating that even thermostable proteins can lend themselves to further stability improvement, our findings provide direct evidence that arginine residues are important stabilizing elements in proteins. Moreover, the stabilizing role of electrostatic interactions, particularly between subunits in oligomeric proteins, is documented.
About this Structure
3XIM is a Single protein structure of sequence from Actinoplanes missouriensis with and as ligands. Active as Xylose isomerase, with EC number 5.3.1.5 Full crystallographic information is available from OCA.
Reference
Arginine residues as stabilizing elements in proteins., Mrabet NT, Van den Broeck A, Van den brande I, Stanssens P, Laroche Y, Lambeir AM, Matthijssens G, Jenkins J, Chiadmi M, van Tilbeurgh H, et al., Biochemistry. 1992 Mar 3;31(8):2239-53. PMID:1540579
Page seeded by OCA on Thu Feb 21 19:11:47 2008
Categories: Actinoplanes missouriensis | Single protein | Xylose isomerase | Brande, I Van Den. | Chiadmi, M. | Demaeyer, M. | Denbroek, A Van. | Janin, J. | Jenkins, J. | Lambeir, A M. | Laroche, Y. | Lasters, I. | Matthyssens, G. | Mrabet, N T. | Quax, W J. | Rey, F. | Stanssens, P. | Vantilbeurgh, H. | Wodak, S J. | CO | SOR | Isomerase(intramolecular oxidoreductse)
