5h3g
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 5h3g is ON HOLD Authors: Kong, G.K.W., Chan, W.H.Y. Description: Crystal Structure of Oryza sativa Acyl-CoA-Binding Protein 1 [[Category: Unrelease...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of Oryza sativa Acyl-CoA-Binding Protein 1== | |
| + | <StructureSection load='5h3g' size='340' side='right'caption='[[5h3g]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5h3g]] is a 1 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=5H3G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5H3G FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=5h3g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h3g OCA], [https://pdbe.org/5h3g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5h3g RCSB], [https://www.ebi.ac.uk/pdbsum/5h3g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5h3g ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ACBP1_ORYSJ ACBP1_ORYSJ] Binds medium- and long-chain acyl-CoA esters with high affinity. Can interact in vitro with palmitoyl-CoA, oleoyl-CoA, linoleoyl-CoA and linolenoyl-CoA (PubMed:21128943). 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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:28471368</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5h3g" style="background-color:#fffaf0;"></div> |
| - | [[Category: Chan | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Oryza sativa Japonica Group]] | ||
| + | [[Category: Chan WHY]] | ||
| + | [[Category: Kong GKW]] | ||
Current revision
Crystal Structure of Oryza sativa Acyl-CoA-Binding Protein 1
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