1lwd
From Proteopedia
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| - | [[Image:1lwd.jpg|left|200px]] | + | [[Image:1lwd.jpg|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF NADP-DEPENDENT ISOCITRATE DEHYDROGENASE FROM PORCINE HEART MITOCHONDRIA''' | + | {{Structure |
| + | |PDB= 1lwd |SIZE=350|CAPTION= <scene name='initialview01'>1lwd</scene>, resolution 1.85Å | ||
| + | |SITE= <scene name='pdbsite=MN1:Active+Site+Of+Isocitrate+Dehydrogenase+Is+Where+Oxidati+...'>MN1</scene> and <scene name='pdbsite=MN2:Active+Site+Of+Isocitrate+Dehydrogenase+Is+Where+Oxidati+...'>MN2</scene> | ||
| + | |LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=ICT:ISOCITRIC ACID'>ICT</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF NADP-DEPENDENT ISOCITRATE DEHYDROGENASE FROM PORCINE HEART MITOCHONDRIA''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1LWD is a [ | + | 1LWD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LWD OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of porcine mitochondrial NADP+-dependent isocitrate dehydrogenase complexed with Mn2+ and isocitrate. Insights into the enzyme mechanism., Ceccarelli C, Grodsky NB, Ariyaratne N, Colman RF, Bahnson BJ, J Biol Chem. 2002 Nov 8;277(45):43454-62. Epub 2002 Aug 30. PMID:[http:// | + | Crystal structure of porcine mitochondrial NADP+-dependent isocitrate dehydrogenase complexed with Mn2+ and isocitrate. Insights into the enzyme mechanism., Ceccarelli C, Grodsky NB, Ariyaratne N, Colman RF, Bahnson BJ, J Biol Chem. 2002 Nov 8;277(45):43454-62. Epub 2002 Aug 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12207025 12207025] |
[[Category: Isocitrate dehydrogenase (NADP(+))]] | [[Category: Isocitrate dehydrogenase (NADP(+))]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: tricarboxylic acid cycle]] | [[Category: tricarboxylic acid cycle]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:36:02 2008'' |
Revision as of 10:36, 20 March 2008
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| , resolution 1.85Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | and | ||||||
| Ligands: | , and | ||||||
| Activity: | Isocitrate dehydrogenase (NADP(+)), with EC number 1.1.1.42 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF NADP-DEPENDENT ISOCITRATE DEHYDROGENASE FROM PORCINE HEART MITOCHONDRIA
Overview
The crystal structure of porcine heart mitochondrial NADP+-dependent isocitrate dehydrogenase (IDH) complexed with Mn2+ and isocitrate was solved to a resolution of 1.85 A. The enzyme was expressed in Escherichia coli, purified as a fusion protein with maltose binding protein, and cleaved with thrombin to yield homogeneous enzyme. The structure was determined by multiwavelength anomalous diffraction phasing using selenium substitution in the form of selenomethionine as the anomalous scatterer. The porcine NADP+-IDH enzyme is structurally compared with the previously solved structures of IDH from E. coli and Bacillus subtilis that share 16 and 17% identity, respectively, with the mammalian enzyme. The porcine enzyme has a protein fold similar to the bacterial IDH structures with each monomer folding into two domains. However, considerable differences exist between the bacterial and mammalian forms of IDH in regions connecting core secondary structure. Based on the alignment of sequence and structure among the porcine, E. coli, and B. subtilis IDH, a putative phosphorylation site has been identified for the mammalian enzyme. The active site, including the bound Mn2+-isocitrate complex, is highly ordered and, therefore, mechanistically informative. The consensus IDH mechanism predicts that the Mn2+-bound hydroxyl of isocitrate is deprotonated prior to its NADP+-dependent oxidation. The present crystal structure has an active site water that is well positioned to accept the proton and ultimately transfer the proton to solvent through an additional bound water.
About this Structure
1LWD is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.
Reference
Crystal structure of porcine mitochondrial NADP+-dependent isocitrate dehydrogenase complexed with Mn2+ and isocitrate. Insights into the enzyme mechanism., Ceccarelli C, Grodsky NB, Ariyaratne N, Colman RF, Bahnson BJ, J Biol Chem. 2002 Nov 8;277(45):43454-62. Epub 2002 Aug 30. PMID:12207025
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