1hb8

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(New page: 200px<br /><applet load="1hb8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hb8, resolution 2.00&Aring;" /> '''STRUCTURE OF BOVINE ...)
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[[Image:1hb8.jpg|left|200px]]<br /><applet load="1hb8" size="350" color="white" frame="true" align="right" spinBox="true"
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caption="1hb8, resolution 2.00&Aring;" />
'''STRUCTURE OF BOVINE ACYL-COA BINDING PROTEIN IN TETRAGONAL CRYSTAL FORM'''<br />
'''STRUCTURE OF BOVINE ACYL-COA BINDING PROTEIN IN TETRAGONAL CRYSTAL FORM'''<br />
==Overview==
==Overview==
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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.
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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==
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1HB8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HB8 OCA].
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1HB8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HB8 OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Bergfors, T.]]
[[Category: Bergfors, T.]]
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[[Category: Jones, T.A.]]
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[[Category: Jones, T A.]]
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[[Category: Kleywegt, G.J.]]
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[[Category: Kleywegt, G J.]]
[[Category: Knudsen, J.]]
[[Category: Knudsen, J.]]
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[[Category: Zou, J.Y.]]
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[[Category: Zou, J Y.]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: acyl-coa]]
[[Category: acyl-coa]]
[[Category: binding protein]]
[[Category: binding protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:29:41 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:59:25 2008''

Revision as of 10:59, 21 February 2008


1hb8, resolution 2.00Å

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STRUCTURE OF BOVINE ACYL-COA BINDING PROTEIN IN TETRAGONAL CRYSTAL FORM

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

1HB8 is a Single protein structure of sequence from [1] with as ligand. 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

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