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2.8-Å crystal structure of Escherichia coli YidC revealing all core regions, including flexible C2 loop

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dc.contributor.author Tanaka, Yoshiki en
dc.contributor.author Tsukazaki, Tomoya en
dc.date.accessioned 2019-05-13T06:12:09Z en
dc.date.available 2019-05-13T06:12:09Z en
dc.date.issued 2018-10-20 en
dc.identifier.issn 0006-291X en
dc.identifier.uri http://hdl.handle.net/10061/13291 en
dc.description.abstract YidC/Alb3/Oxa1 family proteins are involved in the insertion and assembly of membrane proteins. The core five transmembrane regions of YidC, which are conserved in the protein family, form a positively charged cavity open to the cytoplasmic side. The cavity plays an important role in membrane protein insertion. In all reported structural studies of YidC, the second cytoplasmic loop (C2 loop) was disordered, limiting the understanding of its role. Here, we determined the crystal structure of YidC including the C2 loop at 2.8 Å resolution with R/Rfree = 21.8/27.5. This structure and subsequent molecular dynamics simulation indicated that the intrinsic flexible C2 loop covered the positively charged cavity. This crystal structure provides the coordinates of the complete core region including the C2 loop, which is valuable for further analyses of YidC. ja
dc.language.iso en en
dc.publisher Elsevier en
dc.rights © 2018 Elsevier Inc. All rights reserved. ja
dc.rights 出版社許諾条件により、本文は2019年10月20日以降に公開 ja
dc.subject Crystal structure en
dc.subject YidC en
dc.subject Insertase en
dc.subject Chaperone en
dc.subject Membrane protein en
dc.title 2.8-Å crystal structure of Escherichia coli YidC revealing all core regions, including flexible C2 loop ja
dc.type.nii Journal Article en
dc.contributor.transcription タナカ, ヨシキ ja
dc.contributor.transcription ツカザキ, トモヤ ja
dc.contributor.alternative 田中, 良樹 ja
dc.contributor.alternative 塚崎, 智也 ja
dc.textversion author en
dc.identifier.jtitle Biochemical and Biophysical Research Communications en
dc.identifier.volume 505 en
dc.identifier.issue 1 en
dc.identifier.spage 141 en
dc.identifier.epage 145 en
dc.relation.doi 10.1016/j.bbrc.2018.09.043 en
dc.identifier.NAIST-ID 74650169 en
dc.identifier.NAIST-ID 73299737 en
dc.relation.pmid 30241934 en

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