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| | <StructureSection load='5h3i' size='340' side='right'caption='[[5h3i]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='5h3i' size='340' side='right'caption='[[5h3i]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5h3i]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Japanese_rice Japanese rice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H3I OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5H3I FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5h3i]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryza_sativa_Japonica_Group Oryza sativa Japonica Group]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H3I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5H3I FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</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]] 2.302Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5h3g|5h3g]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">OSJNBa0019F11.14, P0541H01.36, Os06g0115300, OsJ_19900 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=39947 Japanese rice])</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=5h3i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h3i OCA], [https://pdbe.org/5h3i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5h3i RCSB], [https://www.ebi.ac.uk/pdbsum/5h3i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5h3i ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5h3i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h3i OCA], [http://pdbe.org/5h3i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h3i RCSB], [http://www.ebi.ac.uk/pdbsum/5h3i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h3i ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/ACBP2_ORYSJ ACBP2_ORYSJ] Binds medium- and long-chain acyl-CoA esters with high affinity. Can interact in vitro with linolenoyl-CoA (PubMed:21128943). Binds palmitoyl-CoA and linoleoyl-CoA in vitro (PubMed:28471368). Binds phosphatidic acid (PA) and phosphatidylcholine (PC) in vitro. May play a role in the biosynthesis of phospholipids (PubMed:24738983).<ref>PMID:21128943</ref> <ref>PMID:24738983</ref> <ref>PMID:28471368</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Japanese rice]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Guo, Z H]] | + | [[Category: Oryza sativa Japonica Group]] |
| - | [[Category: Kong, G K.W]] | + | [[Category: Guo Z-H]] |
| - | [[Category: Acyl-coa-binding domain]]
| + | [[Category: Kong GKW]] |
| - | [[Category: Lipid binding protein]] | + | |
| Structural highlights
Function
ACBP2_ORYSJ Binds medium- and long-chain acyl-CoA esters with high affinity. Can interact in vitro with linolenoyl-CoA (PubMed:21128943). Binds palmitoyl-CoA and linoleoyl-CoA in vitro (PubMed:28471368). Binds phosphatidic acid (PA) and phosphatidylcholine (PC) in vitro. May play a role in the biosynthesis of phospholipids (PubMed:24738983).[1] [2] [3]
Publication Abstract from PubMed
Acyl-CoA-binding proteins (ACBPs) are a family of proteins that facilitate the binding of long-chain acyl-CoA esters at a conserved acyl-CoA-binding domain. ACBPs act to form intracellular acyl-CoA pools, transport acyl-CoA esters and regulate lipid metabolism. In the model plant Arabidopsis thaliana, a family of six ACBPs has been demonstrated to function in stress and development. Six ACBPs (OsACBPs) have also been identified in Oryza sativa (rice), but they are not as well characterized as those in Arabidopsis thaliana. To understand the need in rice for the two 10 kDa ACBPs, namely OsACBP1 and OsACBP2, which share 79% sequence identity, their crystal structures were elucidated and their affinities toward acyl-CoA esters were compared using isothermal titration calorimetry. OsACBP2 was found to display a higher binding affinity for unsaturated acyl-CoA esters than OsACBP1. A difference between the two proteins is observed at helix 3 and is predicted to lead to different ligand-binding modes in terms of the shape of the binding pocket and the residues that are involved. OsACBP1 thus resembles bovine ACBP, while OsACBP2 is similar to human liver ACBP, in both structure and binding affinity. This is the first time that ACBP structures have been reported from plants, and suggests that OsACBP1 and OsACBP2 are not redundant in function despite their high sequence identity and general structural similarity.
The first plant acyl-CoA-binding protein structures: the close homologues OsACBP1 and OsACBP2 from rice.,Guo ZH, Chan WHY, Kong GKW, Hao Q, Chye ML Acta Crystallogr D Struct Biol. 2017 May 1;73(Pt 5):438-448. doi:, 10.1107/S2059798317004193. Epub 2017 Apr 26. PMID:28471368[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Meng W, Su YCF, Saunders RMK, Chye ML. The rice acyl-CoA-binding protein gene family: phylogeny, expression and functional analysis. New Phytol. 2011 Mar;189(4):1170-1184. PMID:21128943 doi:10.1111/j.1469-8137.2010.03546.x
- ↑ Meng W, Hsiao AS, Gao C, Jiang L, Chye ML. Subcellular localization of rice acyl-CoA-binding proteins (ACBPs) indicates that OsACBP6::GFP is targeted to the peroxisomes. New Phytol. 2014 Jul;203(2):469-482. PMID:24738983 doi:10.1111/nph.12809
- ↑ Guo ZH, Chan WHY, Kong GKW, Hao Q, Chye ML. The first plant acyl-CoA-binding protein structures: the close homologues OsACBP1 and OsACBP2 from rice. Acta Crystallogr D Struct Biol. 2017 May 1;73(Pt 5):438-448. doi:, 10.1107/S2059798317004193. Epub 2017 Apr 26. PMID:28471368 doi:http://dx.doi.org/10.1107/S2059798317004193
- ↑ Guo ZH, Chan WHY, Kong GKW, Hao Q, Chye ML. The first plant acyl-CoA-binding protein structures: the close homologues OsACBP1 and OsACBP2 from rice. Acta Crystallogr D Struct Biol. 2017 May 1;73(Pt 5):438-448. doi:, 10.1107/S2059798317004193. Epub 2017 Apr 26. PMID:28471368 doi:http://dx.doi.org/10.1107/S2059798317004193
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