1pjl

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[[Image:1pjl.gif|left|200px]]
[[Image:1pjl.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1pjl |SIZE=350|CAPTION= <scene name='initialview01'>1pjl</scene>, resolution 2.9&Aring;
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The line below this paragraph, containing "STRUCTURE_1pjl", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=LU:LUTETIUM+(III)+ION'>LU</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Malate_dehydrogenase_(oxaloacetate-decarboxylating) Malate dehydrogenase (oxaloacetate-decarboxylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.38 1.1.1.38] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= ME2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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-->
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|DOMAIN=
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{{STRUCTURE_1pjl| PDB=1pjl | SCENE= }}
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|RELATEDENTRY=[[1do8|1DO8]], [[1qr6|1QR6]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pjl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pjl OCA], [http://www.ebi.ac.uk/pdbsum/1pjl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pjl RCSB]</span>
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}}
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'''Crystal structure of human m-NAD-ME in ternary complex with NAD and Lu3+'''
'''Crystal structure of human m-NAD-ME in ternary complex with NAD and Lu3+'''
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Potent and competitive inhibition of malic enzymes by lanthanide ions., Yang Z, Batra R, Floyd DL, Hung HC, Chang GG, Tong L, Biochem Biophys Res Commun. 2000 Aug 2;274(2):440-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10913357 10913357]
Potent and competitive inhibition of malic enzymes by lanthanide ions., Yang Z, Batra R, Floyd DL, Hung HC, Chang GG, Tong L, Biochem Biophys Res Commun. 2000 Aug 2;274(2):440-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10913357 10913357]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Malate dehydrogenase (oxaloacetate-decarboxylating)]]
 
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Batra, R.]]
[[Category: Batra, R.]]
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[[Category: Tong, L.]]
[[Category: Tong, L.]]
[[Category: Yang, Z.]]
[[Category: Yang, Z.]]
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[[Category: oxidoreductase]]
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[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:09:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:00:34 2008''
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Revision as of 02:09, 3 May 2008

Template:STRUCTURE 1pjl

Crystal structure of human m-NAD-ME in ternary complex with NAD and Lu3+


Contents

Overview

The catalytic activity of malic enzyme (ME), a member of a new class of oxidative decarboxylases, requires the presence of divalent cations (Mn(2+), Mg(2+), and others). The crystal structure at 2.9 A resolution of human mitochondrial NAD(+)-dependent malic enzyme in a ternary complex with NAD(+) and the lanthanide ion Lu(3+), which has similar radius as Mn(2+), reveals a new conformation of the enzyme. The active site in this ternary complex is in an open form, while the organization of the tetramer of the enzyme actually resembles that with a closed active site. The Lu(3+) ion is bound to the enzyme at the same site as Mn(2+). Kinetic studies showed that Lu(3+) is a potent inhibitor of both the human NAD(P)(+)-dependent ME and the NADP(+)-dependent ME from pigeon liver, and is competitive with respect to the divalent cation, consistent with the structural information.

Disease

Known disease associated with this structure: Epilepsy, idopathic generalized, susceptibility to OMIM:[154270]

About this Structure

1PJL is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Potent and competitive inhibition of malic enzymes by lanthanide ions., Yang Z, Batra R, Floyd DL, Hung HC, Chang GG, Tong L, Biochem Biophys Res Commun. 2000 Aug 2;274(2):440-4. PMID:10913357 Page seeded by OCA on Sat May 3 05:09:34 2008

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