Tags

Type your tag names separated by a space and hit enter

Purification, crystallization and preliminary structural characterization of the periplasmic domain P1 of the Escherichia coli membrane-protein insertase YidC.

Abstract

In Escherichia coli, the biogenesis of inner membrane proteins (IMPs) requires targeting and insertion factors such as the signal recognition particle (SRP) and the Sec translocon. Recent studies have identified YidC as a novel and essential component involved in membrane insertion of IMPs both in conjunction with the Sec translocon and as a separate entity. E. coli YidC is a member of the YidC (in bacteria)/Oxa1 (in mitochondria)/Alb3 (in chloroplasts) protein family and contains six transmembrane segments and a very large periplasmic domain P1. The overproduction, purification, crystallization and preliminary crystallographic studies of the native and selenomethionine-labelled P1 domain are reported here as a first step towards the elucidation of the molecular mechanism of YidC as a membrane-protein insertase.

Authors+Show Affiliations

Biochemie-Zentrum der Universität Heidelberg (BZH), INF 328, D-69120 Heidelberg, Germany.No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

18259071

Citation

Ravaud, Stephanie, et al. "Purification, Crystallization and Preliminary Structural Characterization of the Periplasmic Domain P1 of the Escherichia Coli Membrane-protein Insertase YidC." Acta Crystallographica. Section F, Structural Biology and Crystallization Communications, vol. 64, no. Pt 2, 2008, pp. 144-8.
Ravaud S, Wild K, Sinning I. Purification, crystallization and preliminary structural characterization of the periplasmic domain P1 of the Escherichia coli membrane-protein insertase YidC. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008;64(Pt 2):144-8.
Ravaud, S., Wild, K., & Sinning, I. (2008). Purification, crystallization and preliminary structural characterization of the periplasmic domain P1 of the Escherichia coli membrane-protein insertase YidC. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications, 64(Pt 2), pp. 144-8. doi:10.1107/S1744309108002364.
Ravaud S, Wild K, Sinning I. Purification, Crystallization and Preliminary Structural Characterization of the Periplasmic Domain P1 of the Escherichia Coli Membrane-protein Insertase YidC. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Feb 1;64(Pt 2):144-8. PubMed PMID: 18259071.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Purification, crystallization and preliminary structural characterization of the periplasmic domain P1 of the Escherichia coli membrane-protein insertase YidC. AU - Ravaud,Stephanie, AU - Wild,Klemens, AU - Sinning,Irmgard, Y1 - 2008/01/31/ PY - 2007/12/20/received PY - 2008/01/22/accepted PY - 2008/2/9/pubmed PY - 2008/8/8/medline PY - 2008/2/9/entrez SP - 144 EP - 8 JF - Acta crystallographica. Section F, Structural biology and crystallization communications JO - Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. VL - 64 IS - Pt 2 N2 - In Escherichia coli, the biogenesis of inner membrane proteins (IMPs) requires targeting and insertion factors such as the signal recognition particle (SRP) and the Sec translocon. Recent studies have identified YidC as a novel and essential component involved in membrane insertion of IMPs both in conjunction with the Sec translocon and as a separate entity. E. coli YidC is a member of the YidC (in bacteria)/Oxa1 (in mitochondria)/Alb3 (in chloroplasts) protein family and contains six transmembrane segments and a very large periplasmic domain P1. The overproduction, purification, crystallization and preliminary crystallographic studies of the native and selenomethionine-labelled P1 domain are reported here as a first step towards the elucidation of the molecular mechanism of YidC as a membrane-protein insertase. SN - 1744-3091 UR - https://www.unboundmedicine.com/medline/citation/18259071/Purification_crystallization_and_preliminary_structural_characterization_of_the_periplasmic_domain_P1_of_the_Escherichia_coli_membrane_protein_insertase_YidC_ L2 - http://scripts.iucr.org/cgi-bin/paper?S1744309108002364 DB - PRIME DP - Unbound Medicine ER -