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Article: Crystal structure of the rice acyl‐CoA‐binding protein OsACBP2 in complex with C18:3‐CoA reveals a novel pattern of binding to acyl‐CoA esters

TitleCrystal structure of the rice acyl‐CoA‐binding protein OsACBP2 in complex with C18:3‐CoA reveals a novel pattern of binding to acyl‐CoA esters
Authors
Keywordsacyl-CoA binding
multiangle light scattering
Oryza sativa
protein–lipid interaction
X-ray diffraction
Issue Date2020
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febslet
Citation
FEBS Letters, 2020, v. 594 n. 21, p. 3568-3575 How to Cite?
AbstractAcyl-CoA-binding proteins (ACBPs) are a family of proteins that bind acyl-CoA esters at a conserved acyl-CoA-binding domain. ACBPs maintain intracellular acyl-CoA pools to regulate lipid metabolism. Here, we report on the structure of rice OsACBP2 in complex with C18:3-CoA ester. The residues Y33, K34 and K56 of OsACBP2 play a crucial role in binding the CoA group, while residues N23, L27, K52 and Y55 in one molecule of OsACBP2 cooperate with L27, L28, A59 and A62 from another anchoring the fatty acyl group. Multiangle light scattering assays indicate that OsACBP2 binds C18:3-CoA as a monomer. The first complex structure of a plant ACBP binding with C18:3-CoA is therefore presented, providing a novel model for the interaction between an acyl-CoA ester and the acyl-CoA-binding domain(s).
Persistent Identifierhttp://hdl.handle.net/10722/295891
ISSN
2020 Impact Factor: 4.124
2015 SCImago Journal Rankings: 2.026
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorJin, J-
dc.contributor.authorGuo, ZH-
dc.contributor.authorHao, Q-
dc.contributor.authorChye, ML-
dc.date.accessioned2021-02-08T08:15:30Z-
dc.date.available2021-02-08T08:15:30Z-
dc.date.issued2020-
dc.identifier.citationFEBS Letters, 2020, v. 594 n. 21, p. 3568-3575-
dc.identifier.issn0014-5793-
dc.identifier.urihttp://hdl.handle.net/10722/295891-
dc.description.abstractAcyl-CoA-binding proteins (ACBPs) are a family of proteins that bind acyl-CoA esters at a conserved acyl-CoA-binding domain. ACBPs maintain intracellular acyl-CoA pools to regulate lipid metabolism. Here, we report on the structure of rice OsACBP2 in complex with C18:3-CoA ester. The residues Y33, K34 and K56 of OsACBP2 play a crucial role in binding the CoA group, while residues N23, L27, K52 and Y55 in one molecule of OsACBP2 cooperate with L27, L28, A59 and A62 from another anchoring the fatty acyl group. Multiangle light scattering assays indicate that OsACBP2 binds C18:3-CoA as a monomer. The first complex structure of a plant ACBP binding with C18:3-CoA is therefore presented, providing a novel model for the interaction between an acyl-CoA ester and the acyl-CoA-binding domain(s).-
dc.languageeng-
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febslet-
dc.relation.ispartofFEBS Letters-
dc.subjectacyl-CoA binding-
dc.subjectmultiangle light scattering-
dc.subjectOryza sativa-
dc.subjectprotein–lipid interaction-
dc.subjectX-ray diffraction-
dc.titleCrystal structure of the rice acyl‐CoA‐binding protein OsACBP2 in complex with C18:3‐CoA reveals a novel pattern of binding to acyl‐CoA esters-
dc.typeArticle-
dc.identifier.emailJin, J: jinjing@hku.hk-
dc.identifier.emailGuo, ZH: zhguo1990@hku.hk-
dc.identifier.emailHao, Q: qhao@hku.hk-
dc.identifier.emailChye, ML: mlchye@hku.hk-
dc.identifier.authorityHao, Q=rp01332-
dc.identifier.authorityChye, ML=rp00687-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1002/1873-3468.13923-
dc.identifier.pmid32888212-
dc.identifier.hkuros321231-
dc.identifier.hkuros322519-
dc.identifier.volume594-
dc.identifier.issue21-
dc.identifier.spage3568-
dc.identifier.epage3575-
dc.identifier.isiWOS:000570297800001-
dc.publisher.placeNetherlands-

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