Sandbox Reserved 1094: Difference between revisions

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== Evolutionary conservation ==

The different structures conserved evolutionary can be observed according to the scale following.

[[Image:Consurf_key_small.gif|200px|right]]

Check<jmol>

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Depending on several conditions, it can dimerize to form tetramers. Each monomer in the complex has a substrate binding site that binds to G6P, and a catalytic coenzyme binding site that binds to NADP+/NADPH using the Rossman fold.

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. Y

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein.

</StructureSection>

== References ==

~~3. Ravera S., Calzia D., Morelli A. et Panfoli I. 2010. Oligomerization studies of Leuconostoc mesenteroides G6PD activity after SDS-PAGE and blotting. Molekuliarnaia Biologiia. 44(3):472-6.~~

~~4. Cosgrove MS., Naylor C., Paludan S., Adams MJ. et Levy HR. 1998. On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase. Biochemistry. 37(9):2759-67.~~

5. Cosgrove MS., Loh SN., Ha JH. et Levy HR. 2002. The catalytic mechanism of glucose 6-phosphate dehydrogenases: assignment and 1H NMR spectroscopy pH titration of the catalytic histidine residue in the 109 kDa Leuconostoc mesenteroides enzyme. Biochemistry. 41(22):6939-45.

~~6. Rowland P, Basak AK, Gover S, Levy HR, Adams MJ. The three-dimensional structure of glucose 6-phosphate dehydrogenase from Leuconostoc~~

~~mesenteroides refined at 2.0 A resolution. Structure. 1994 Nov 15;2(11):1073-87.~~

== Proteopedia page contributors and editors ==

DONATI Quentin, LOGEREAU Lucie, PROST Loana

Sandbox Reserved 1094: Difference between revisions

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@@ Line 22: / Line 22: @@
 == Evolutionary conservation ==
 The different structures conserved evolutionary can be observed according to the scale following.
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
@@ Line 41: / Line 40: @@
 Depending on several conditions, it can dimerize to form tetramers. Each monomer in the complex has a substrate binding site that binds to G6P, and a catalytic coenzyme binding site that binds to NADP+/NADPH using the Rossman fold.
-This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. Y
+This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein.
 </StructureSection>
 == References ==
 <references/>
-. Ravera S., Calzia D., Morelli A. et Panfoli I. 2010. Oligomerization studies of Leuconostoc mesenteroides G6PD activity after SDS-PAGE and blotting. Molekuliarnaia Biologiia. 44(3):472-6.
-. Cosgrove MS., Naylor C., Paludan S., Adams MJ. et Levy HR. 1998. On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase. Biochemistry. 37(9):2759-67.
-. Cosgrove MS., Loh SN., Ha JH. et Levy HR. 2002. The catalytic mechanism of glucose 6-phosphate dehydrogenases: assignment and 1H NMR spectroscopy pH titration of the catalytic histidine residue in the 109 kDa Leuconostoc mesenteroides enzyme. Biochemistry. 41(22):6939-45.
-. Rowland P, Basak AK, Gover S, Levy HR, Adams MJ. The three-dimensional structure of glucose 6-phosphate dehydrogenase from Leuconostoc
-mesenteroides refined at 2.0 A resolution. Structure. 1994 Nov 15;2(11):1073-87.
 == Proteopedia page contributors and editors ==
 DONATI Quentin, LOGEREAU Lucie, PROST Loana