1hbk
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Acyl-CoA binding protein (ACBP) maintains a pool of fatty acyl-CoA, molecules in the cell and plays a role in fatty acid metabolism. The, biochemical properties of Plasmodium falciparum ACBP are described, together with the 2.0 A resolution crystal structures of a P. falciparum, ACBP-acyl-CoA complex and of bovine ACBP in two crystal forms. Overall, the bovine ACBP crystal structures are similar to the NMR structures, published previously; however, the bovine and parasite ACBP structures are, less similar. The parasite ACBP is shown to have a different, ligand-binding pocket, leading to an acyl-CoA binding specificity, different from that of bovine ACBP. Several non-conservative differences, in residues that interact with the ligand were identified between the, mammalian and parasite .. | + | Acyl-CoA binding protein (ACBP) maintains a pool of fatty acyl-CoA, molecules in the cell and plays a role in fatty acid metabolism. The, biochemical properties of Plasmodium falciparum ACBP are described, together with the 2.0 A resolution crystal structures of a P. falciparum, ACBP-acyl-CoA complex and of bovine ACBP in two crystal forms. Overall, the bovine ACBP crystal structures are similar to the NMR structures, published previously; however, the bovine and parasite ACBP structures are, less similar. The parasite ACBP is shown to have a different, ligand-binding pocket, leading to an acyl-CoA binding specificity, different from that of bovine ACBP. Several non-conservative differences, in residues that interact with the ligand were identified between the, mammalian and parasite ACBPs. These, together with measured, binding-specificity differences, suggest that there is a potential for the, design of molecules that might selectively block the acyl-CoA binding, site. |
==About this Structure== | ==About this Structure== | ||
| - | 1HBK is a | + | 1HBK is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum] with NI, COA and MYR as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Sites: COA, MYR, NI1 and NI2. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HBK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: fatty acid metabolism]] | [[Category: fatty acid metabolism]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 12:45:50 2007'' |
Revision as of 10:40, 5 November 2007
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ACYL-COA BINDING PROTEIN FROM PLASMODIUM FALCIPARUM
Overview
Acyl-CoA binding protein (ACBP) maintains a pool of fatty acyl-CoA, molecules in the cell and plays a role in fatty acid metabolism. The, biochemical properties of Plasmodium falciparum ACBP are described, together with the 2.0 A resolution crystal structures of a P. falciparum, ACBP-acyl-CoA complex and of bovine ACBP in two crystal forms. Overall, the bovine ACBP crystal structures are similar to the NMR structures, published previously; however, the bovine and parasite ACBP structures are, less similar. The parasite ACBP is shown to have a different, ligand-binding pocket, leading to an acyl-CoA binding specificity, different from that of bovine ACBP. Several non-conservative differences, in residues that interact with the ligand were identified between the, mammalian and parasite ACBPs. These, together with measured, binding-specificity differences, suggest that there is a potential for the, design of molecules that might selectively block the acyl-CoA binding, site.
About this Structure
1HBK is a Protein complex structure of sequences from Plasmodium falciparum with NI, COA and MYR as ligands. Structure known Active Sites: COA, MYR, NI1 and NI2. Full crystallographic information is available from OCA.
Reference
Binding site differences revealed by crystal structures of Plasmodium falciparum and bovine acyl-CoA binding protein., van Aalten DM, Milne KG, Zou JY, Kleywegt GJ, Bergfors T, Ferguson MA, Knudsen J, Jones TA, J Mol Biol. 2001 May 25;309(1):181-92. PMID:11491287
Page seeded by OCA on Mon Nov 5 12:45:50 2007
