1evj: Difference between revisions
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=" | [[Image:1evj.gif|left|200px]]<br /><applet load="1evj" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1evj, resolution 2.70Å" /> | caption="1evj, resolution 2.70Å" /> | ||
'''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 | 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:// | 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 | [[Category: Baker, E N.]] | ||
[[Category: Baker, H | [[Category: Baker, H M.]] | ||
[[Category: Halbig, D.]] | [[Category: Halbig, D.]] | ||
[[Category: Hardman, M | [[Category: Hardman, M J.]] | ||
[[Category: Lott, J | [[Category: Lott, J S.]] | ||
[[Category: Sprenger, G | [[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:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:31:56 2008'' | ||
Revision as of 13:31, 21 February 2008
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CRYSTAL STRUCTURE OF GLUCOSE-FRUCTOSE OXIDOREDUCTASE (GFOR) DELTA1-22 S64D
OverviewOverview
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 StructureAbout this Structure
1EVJ is a Single protein structure of sequence from Zymomonas mobilis with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of a truncated mutant of glucose-fructose oxidoreductase shows that an N-terminal arm controls tetramer formation., Lott JS, Halbig D, Baker HM, Hardman MJ, Sprenger GA, Baker EN, J Mol Biol. 2000 Dec 8;304(4):575-84. PMID:11099381
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