1gz3: Difference between revisions

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[[Image:1gz3.~~jpg~~|left|200px]]

[[Image:1gz3.png|left|200px]]

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~~'''~~MOLECULAR MECHANISM FOR THE REGULATION OF HUMAN MITOCHONDRIAL NAD(P)+-DEPENDENT MALIC ENZYME BY ATP AND FUMARATE~~'''~~

===MOLECULAR MECHANISM FOR THE REGULATION OF HUMAN MITOCHONDRIAL NAD(P)+-DEPENDENT MALIC ENZYME BY ATP AND FUMARATE===

~~==Overview==~~

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The ~~regulation of human mitochondrial NAD(P)+-dependent malic enzyme (m-NAD-ME) by ATP and fumarate may be crucial for~~ the ~~metabolism of glutamine for energy production in rapidly proliferating tissues and tumors. Here we report~~ the ~~crystal structure~~ at 2.~~2 A resolution of m-NAD-ME in complex with ATP, Mn2+, tartronate, and fumarate~~. ~~Our structural~~, ~~kinetic, and mutagenesis studies reveal unexpectedly that ATP~~ is ~~an active-site inhibitor of the enzyme, despite~~ the presence of an exo binding site. The structure also reveals the allosteric binding site for fumarate in the dimer interface. Mutations in this binding site abolished the activating effects of fumarate. Comparison to the structure in the absence of fumarate indicates a possible molecular mechanism for the allosteric function of this compound.

The line below this paragraph, {{ABSTRACT_PUBMED_12121650}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12121650 is the PubMed ID number.

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==About this Structure==

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[[Category: Oxidoreductase]]

[[Category: Protein structure]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 18~~:12:08 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:20:51 2008''

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-[[Image:1gz3.jpg|left|200px]]
+{{Seed}}
+[[Image:1gz3.png|left|200px]]
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 {{STRUCTURE_1gz3|  PDB=1gz3  |  SCENE=  }}
-'''MOLECULAR MECHANISM FOR THE REGULATION OF HUMAN MITOCHONDRIAL NAD(P)+-DEPENDENT MALIC ENZYME BY ATP AND FUMARATE'''
+===MOLECULAR MECHANISM FOR THE REGULATION OF HUMAN MITOCHONDRIAL NAD(P)+-DEPENDENT MALIC ENZYME BY ATP AND FUMARATE===
-==Overview==
+<!--
-The regulation of human mitochondrial NAD(P)+-dependent malic enzyme (m-NAD-ME) by ATP and fumarate may be crucial for the metabolism of glutamine for energy production in rapidly proliferating tissues and tumors. Here we report the crystal structure at 2.2 A resolution of m-NAD-ME in complex with ATP, Mn2+, tartronate, and fumarate. Our structural, kinetic, and mutagenesis studies reveal unexpectedly that ATP is an active-site inhibitor of the enzyme, despite the presence of an exo binding site. The structure also reveals the allosteric binding site for fumarate in the dimer interface. Mutations in this binding site abolished the activating effects of fumarate. Comparison to the structure in the absence of fumarate indicates a possible molecular mechanism for the allosteric function of this compound.
+The line below this paragraph, {{ABSTRACT_PUBMED_12121650}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12121650 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12121650}}
 ==About this Structure==
@@ Line 32: / Line 36: @@
 [[Category: Oxidoreductase]]
 [[Category: Protein structure]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 18:12:08 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 06:20:51 2008''