1oc4: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 1oc4 |SIZE=350|CAPTION= <scene name='initialview01'>1oc4</scene>, resolution 2.30Å | |PDB= 1oc4 |SIZE=350|CAPTION= <scene name='initialview01'>1oc4</scene>, resolution 2.30Å | ||
|SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+B'>AC1</scene> | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=OXM:OXAMIC+ACID'>OXM</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/L-lactate_dehydrogenase L-lactate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.27 1.1.1.27] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/L-lactate_dehydrogenase L-lactate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.27 1.1.1.27] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oc4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oc4 OCA], [http://www.ebi.ac.uk/pdbsum/1oc4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1oc4 RCSB]</span> | |||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Brady, L.]] | [[Category: Brady, L.]] | ||
[[Category: Winter, V.]] | [[Category: Winter, V.]] | ||
[[Category: 3-layer (aba) sandwich]] | [[Category: 3-layer (aba) sandwich]] | ||
[[Category: glycolysis]] | [[Category: glycolysis]] | ||
| Line 34: | Line 34: | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:43:01 2008'' | ||
Revision as of 22:43, 30 March 2008
| |||||||
| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , | ||||||
| Activity: | L-lactate dehydrogenase, with EC number 1.1.1.27 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
LACTATE DEHYDROGENASE FROM PLASMODIUM BERGHEI
OverviewOverview
As Plasmodium rely extensively on homolactic fermentation for energy production, Plasmodium falciparum lactate dehydrogenase (PfLDH)--the key enzyme in this process--has previously been suggested as a novel target for antimalarials. This enzyme has distinctive kinetic and structural properties that distinguish it from its human homologues. In this study, we now describe the expression, kinetic characterisation and crystal structure determination of the LDH from Plasmodium berghei. This enzyme is seen to have a similar kinetic profile to its P. falciparum counterpart, exhibiting the characteristic lack of substrate inhibition that distinguishes plasmodial from human LDHs. The crystal structure of P. berghei lactate dehydrogenase (PbLDH) shows a very similar active site arrangement to the P. falciparum enzyme. In particular, an insertion of five amino acid residues in the active site loop creates an enlarged volume in the substrate binding site, and characteristic changes in the residues lining the NADH cofactor binding pocket result in displacement of the cofactor relative to its observed position in mammalian and all other LDH structures. These results imply the special features previously described for PfLDH may be shared across the Plasmodium genus, supporting the universal application of therapeutics targeting this enzyme.
About this StructureAbout this Structure
1OC4 is a Single protein structure of sequence from Plasmodium berghei. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of Plasmodium berghei lactate dehydrogenase indicates the unique structural differences of these enzymes are shared across the Plasmodium genus., Winter VJ, Cameron A, Tranter R, Sessions RB, Brady RL, Mol Biochem Parasitol. 2003 Sep;131(1):1-10. PMID:12967707
Page seeded by OCA on Sun Mar 30 22:43:01 2008