Solution NMR assignment of LpoB, an outer-membrane anchored Penicillin-Binding Protein activator from Escherichia coli.
Solution NMR assignment of LpoB, an outer-membrane anchored Penicillin-Binding Protein activator from Escherichia coli.
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DOI:
10.1007/s12104-014-9557-z
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发表时间:
2015-04
影响因子:
0.9
通讯作者:
Simorre, Jean-Pierre
中科院分区:
文献类型:
--
作者:
Jean, Nicolas L.;Bougault, Catherine M.;Egan, Alexander J. F.;Vollmer, Waldemar;Simorre, Jean-Pierre
关键词:
Bacteria surround their cytoplasmic membrane with the essential heteropolymer peptidoglycan (PG), which is made of glycan chains cross-linked by short peptides, to maintain osmotic stability and cell shape. PG is assembled from lipid II precursor by glycosyltransferase and transpeptidase reactions catalyzed by PG synthases, which are anchored to the cytoplasmic membrane and are controlled from inside the cell by cytoskeletal elements. Recently, two lipoproteins, LpoA and LpoB, were shown to be required in Escherichia coli for activating the main peptidoglycan synthases, Penicillin-Binding Proteins 1A and 1B, from the outer membrane. Here we present the backbone and side-chain assignment of the 1H, 13C and 15N resonances of LpoB from E. coli. We also provide evidence for a two-domain organization of LpoB and a largely disordered, 64 amino acid-long N-terminal domain.
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影响因子:
2.2
作者:
Lescop, Ewen;Kern, Thomas;Brutscher, Bernhard
通讯作者:
Brutscher, Bernhard
影响因子:
64.5
作者:
Paradis-Bleau C;Markovski M;Uehara T;Lupoli TJ;Walker S;Kahne DE;Bernhardt TG
通讯作者:
Bernhardt TG
影响因子:
2.9
作者:
Vranken, WF;Boucher, W;Laue, ED
通讯作者:
Laue, ED
DOI:
10.1073/pnas.0904030106
发表时间:
2009-06-02
影响因子:
11.1
作者:
Sung, Ming-Ta;Lai, Yen-Ting;Ma, Che
通讯作者:
Ma, Che
DOI:
10.1038/nrmicro2677
发表时间:
2011-12-28
期刊:
Nature reviews. Microbiology
影响因子:
--
作者:
Typas A;Banzhaf M;Gross CA;Vollmer W
通讯作者:
Vollmer W