|
|
| (2 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==Structure of bovine Acyl-CoA binding protein in tetragonal crystal form== | | ==Structure of bovine Acyl-CoA binding protein in tetragonal crystal form== |
| - | <StructureSection load='1hb8' size='340' side='right' caption='[[1hb8]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='1hb8' size='340' side='right'caption='[[1hb8]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1hb8]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HB8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HB8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1hb8]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HB8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HB8 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1aca|1aca]], [[2abd|2abd]], [[1hb6|1hb6]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hb8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hb8 OCA], [http://pdbe.org/1hb8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hb8 RCSB], [http://www.ebi.ac.uk/pdbsum/1hb8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hb8 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hb8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hb8 OCA], [https://pdbe.org/1hb8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hb8 RCSB], [https://www.ebi.ac.uk/pdbsum/1hb8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hb8 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ACBP_BOVIN ACBP_BOVIN]] Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. It is also able to displace diazepam from the benzodiazepine (BZD) recognition site located on the GABA type A receptor. It is therefore possible that this protein also acts as a neuropeptide to modulate the action of the GABA receptor.<ref>PMID:11491287</ref> | + | [https://www.uniprot.org/uniprot/ACBP_BOVIN ACBP_BOVIN] Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. It is also able to displace diazepam from the benzodiazepine (BZD) recognition site located on the GABA type A receptor. It is therefore possible that this protein also acts as a neuropeptide to modulate the action of the GABA receptor.<ref>PMID:11491287</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 33: |
Line 33: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bergfors, T]] | + | [[Category: Bos taurus]] |
| - | [[Category: Jones, T A]] | + | [[Category: Large Structures]] |
| - | [[Category: Kleywegt, G J]] | + | [[Category: Bergfors T]] |
| - | [[Category: Knudsen, J]] | + | [[Category: Jones TA]] |
| - | [[Category: Zou, J Y]] | + | [[Category: Kleywegt GJ]] |
| - | [[Category: Acyl-coa]] | + | [[Category: Knudsen J]] |
| - | [[Category: Acyl-coenzyme a binding protein]] | + | [[Category: Zou JY]] |
| - | [[Category: Binding protein]]
| + | |
| Structural highlights
Function
ACBP_BOVIN Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. It is also able to displace diazepam from the benzodiazepine (BZD) recognition site located on the GABA type A receptor. It is therefore possible that this protein also acts as a neuropeptide to modulate the action of the GABA receptor.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ van Aalten DM, Milne KG, Zou JY, Kleywegt GJ, Bergfors T, Ferguson MA, Knudsen J, Jones TA. Binding site differences revealed by crystal structures of Plasmodium falciparum and bovine acyl-CoA binding protein. J Mol Biol. 2001 May 25;309(1):181-92. PMID:11491287 doi:10.1006/jmbi.2001.4749
- ↑ van Aalten DM, Milne KG, Zou JY, Kleywegt GJ, Bergfors T, Ferguson MA, Knudsen J, Jones TA. Binding site differences revealed by crystal structures of Plasmodium falciparum and bovine acyl-CoA binding protein. J Mol Biol. 2001 May 25;309(1):181-92. PMID:11491287 doi:10.1006/jmbi.2001.4749
|
