1oc4
From Proteopedia
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| - | [[Image:1oc4.gif|left|200px]]<br /> | + | [[Image:1oc4.gif|left|200px]]<br /><applet load="1oc4" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1oc4" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1oc4, resolution 2.30Å" /> | caption="1oc4, resolution 2.30Å" /> | ||
'''LACTATE DEHYDROGENASE FROM PLASMODIUM BERGHEI'''<br /> | '''LACTATE DEHYDROGENASE FROM PLASMODIUM BERGHEI'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1OC4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Plasmodium_berghei Plasmodium berghei] with NAD, OXM and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] | + | 1OC4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Plasmodium_berghei Plasmodium berghei] with NAD, OXM and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Known structural/functional Site: <scene name='pdbsite=AC1:Gol Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OC4 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 17:23:09 2007'' |
Revision as of 15:13, 18 December 2007
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LACTATE DEHYDROGENASE FROM PLASMODIUM BERGHEI
Overview
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 Structure
1OC4 is a Single protein structure of sequence from Plasmodium berghei with NAD, OXM and GOL as ligands. Active as L-lactate dehydrogenase, with EC number 1.1.1.27 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
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
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