1itw: Difference between revisions

Revision as of 14:15, 21 February 2008

Crystal structure of the monomeric isocitrate dehydrogenase in complex with isocitrate and Mn

OverviewOverview

NADP(+)-dependent isocitrate dehydrogenase is a member of the beta-decarboxylating dehydrogenase family and catalyzes the oxidative decarboxylation reaction from 2R,3S-isocitrate to yield 2-oxoglutarate and CO(2) in the Krebs cycle. Although most prokaryotic NADP(+)-dependent isocitrate dehydrogenases (IDHs) are homodimeric enzymes, the monomeric IDH with a molecular weight of 80-100 kDa has been found in a few species of bacteria. The 1.95 A crystal structure of the monomeric IDH revealed that it consists of two distinct domains, and its folding topology is related to the dimeric IDH. The structure of the large domain repeats a motif observed in the dimeric IDH. Such a fusional structure by domain duplication enables a single polypeptide chain to form a structure at the catalytic site that is homologous to the dimeric IDH, the catalytic site of which is located at the interface of two identical subunits.

About this StructureAbout this Structure

1ITW is a Single protein structure of sequence from Azotobacter vinelandii with and as ligands. Active as Isocitrate dehydrogenase (NADP(+)), with EC number 1.1.1.42 Full crystallographic information is available from OCA.

ReferenceReference

Structure of the monomeric isocitrate dehydrogenase: evidence of a protein monomerization by a domain duplication., Yasutake Y, Watanabe S, Yao M, Takada Y, Fukunaga N, Tanaka I, Structure. 2002 Dec;10(12):1637-48. PMID:12467571

Page seeded by OCA on Thu Feb 21 13:15:35 2008

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OCA

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-[[Image:1itw.jpg|left|200px]]<br /><applet load="1itw" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1itw.jpg|left|200px]]<br /><applet load="1itw" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1itw, resolution 1.95&Aring;" />
 '''Crystal structure of the monomeric isocitrate dehydrogenase in complex with isocitrate and Mn'''<br />
 ==Overview==
-NADP(+)-dependent isocitrate dehydrogenase is a member of the, beta-decarboxylating dehydrogenase family and catalyzes the oxidative, decarboxylation reaction from 2R,3S-isocitrate to yield 2-oxoglutarate and, CO(2) in the Krebs cycle. Although most prokaryotic NADP(+)-dependent, isocitrate dehydrogenases (IDHs) are homodimeric enzymes, the monomeric, IDH with a molecular weight of 80-100 kDa has been found in a few species, of bacteria. The 1.95 A crystal structure of the monomeric IDH revealed, that it consists of two distinct domains, and its folding topology is, related to the dimeric IDH. The structure of the large domain repeats a, motif observed in the dimeric IDH. Such a fusional structure by domain, duplication enables a single polypeptide chain to form a structure at the, catalytic site that is homologous to the dimeric IDH, the catalytic site, of which is located at the interface of two identical subunits.
+NADP(+)-dependent isocitrate dehydrogenase is a member of the beta-decarboxylating dehydrogenase family and catalyzes the oxidative decarboxylation reaction from 2R,3S-isocitrate to yield 2-oxoglutarate and CO(2) in the Krebs cycle. Although most prokaryotic NADP(+)-dependent isocitrate dehydrogenases (IDHs) are homodimeric enzymes, the monomeric IDH with a molecular weight of 80-100 kDa has been found in a few species of bacteria. The 1.95 A crystal structure of the monomeric IDH revealed that it consists of two distinct domains, and its folding topology is related to the dimeric IDH. The structure of the large domain repeats a motif observed in the dimeric IDH. Such a fusional structure by domain duplication enables a single polypeptide chain to form a structure at the catalytic site that is homologous to the dimeric IDH, the catalytic site of which is located at the interface of two identical subunits.
 ==About this Structure==
-ITW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii] with MN and ICT as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Isocitrate_dehydrogenase_(NADP(+)) Isocitrate dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.42 1.1.1.42] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ITW OCA].
+ITW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii] with <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=ICT:'>ICT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Isocitrate_dehydrogenase_(NADP(+)) Isocitrate dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.42 1.1.1.42] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ITW OCA].
 ==Reference==
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 [[Category: greece key motif]]
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