1evj: Difference between revisions

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New page: left|200px<br /><applet load="1evj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1evj, resolution 2.70Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1evj.gif|left|200px]]<br /><applet load="1evj" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1evj.gif|left|200px]]<br /><applet load="1evj" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1evj, resolution 2.70&Aring;" />
caption="1evj, resolution 2.70&Aring;" />
'''CRYSTAL STRUCTURE OF GLUCOSE-FRUCTOSE OXIDOREDUCTASE (GFOR) DELTA1-22 S64D'''<br />
'''CRYSTAL STRUCTURE OF GLUCOSE-FRUCTOSE OXIDOREDUCTASE (GFOR) DELTA1-22 S64D'''<br />


==Overview==
==Overview==
N-terminal or C-terminal arms that extend from folded protein domains can, play a critical role in quaternary structure and other intermolecular, associations and/or in controlling biological activity. We have tested the, role of an extended N-terminal arm in the structure and function of a, periplasmic enzyme glucose-fructose oxidoreductase (GFOR) from Zymomonas, mobilis. We have determined the crystal structure of the NAD(+) complex of, a truncated form of the enzyme, GFORDelta, in which the first 22 residues, of the N-terminal arm of the mature protein have been deleted. The, structure, refined at 2.7 A resolution (R(cryst)=24.1%, R(free)=28.4%), shows that the truncated form of the enzyme forms a dimer and implies that, the N-terminal arm is essential for tetramer formation by wild-type GFOR., Truncation of the N-terminal arm also greatly increases the solvent, exposure of the cofactor; since GFOR activity is dependent on retention of, the cofactor during the catalytic cycle we conclude that the absence of, GFOR activity in this mutant results from dissociation of the cofactor., The N-terminal arm thus determines the quaternary structure and the, retention of the cofactor for GFOR activity and during translocation into, the periplasm. The structure of GFORDelta also shows how an additional, mutation, Ser64Asp, converts the strict NADP(+) specificity of wild-type, GFOR to a dual NADP(+)/NAD(+) specificity.
N-terminal or C-terminal arms that extend from folded protein domains can play a critical role in quaternary structure and other intermolecular associations and/or in controlling biological activity. We have tested the role of an extended N-terminal arm in the structure and function of a periplasmic enzyme glucose-fructose oxidoreductase (GFOR) from Zymomonas mobilis. We have determined the crystal structure of the NAD(+) complex of a truncated form of the enzyme, GFORDelta, in which the first 22 residues of the N-terminal arm of the mature protein have been deleted. The structure, refined at 2.7 A resolution (R(cryst)=24.1%, R(free)=28.4%), shows that the truncated form of the enzyme forms a dimer and implies that the N-terminal arm is essential for tetramer formation by wild-type GFOR. Truncation of the N-terminal arm also greatly increases the solvent exposure of the cofactor; since GFOR activity is dependent on retention of the cofactor during the catalytic cycle we conclude that the absence of GFOR activity in this mutant results from dissociation of the cofactor. The N-terminal arm thus determines the quaternary structure and the retention of the cofactor for GFOR activity and during translocation into the periplasm. The structure of GFORDelta also shows how an additional mutation, Ser64Asp, converts the strict NADP(+) specificity of wild-type GFOR to a dual NADP(+)/NAD(+) specificity.


==About this Structure==
==About this Structure==
1EVJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Zymomonas_mobilis Zymomonas mobilis] with NAD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EVJ OCA].  
1EVJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Zymomonas_mobilis Zymomonas mobilis] with <scene name='pdbligand=NAD:'>NAD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EVJ OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Zymomonas mobilis]]
[[Category: Zymomonas mobilis]]
[[Category: Baker, E.N.]]
[[Category: Baker, E N.]]
[[Category: Baker, H.M.]]
[[Category: Baker, H M.]]
[[Category: Halbig, D.]]
[[Category: Halbig, D.]]
[[Category: Hardman, M.J.]]
[[Category: Hardman, M J.]]
[[Category: Lott, J.S.]]
[[Category: Lott, J S.]]
[[Category: Sprenger, G.A.]]
[[Category: Sprenger, G A.]]
[[Category: NAD]]
[[Category: NAD]]
[[Category: n-terminal arm]]
[[Category: n-terminal arm]]
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[[Category: periplasm]]
[[Category: periplasm]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:21:22 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:31:56 2008''