Molecular organization of the E. coli cellulose synthase macrocomplex.
Molecular organization of the E. coli cellulose synthase macrocomplex.
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大肠杆菌的分子组织。大肠杆菌纤维素合成酶大复合物。
DOI:
10.1038/s41594-021-00569-7
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发表时间:
2021-03
影响因子:
16.8
通讯作者:
Zimmer, Jochen
中科院分区:
文献类型:
--
作者:
Acheson, Justin F.;Ho, Ruoya;Goularte, Nicolette F.;Cegelski, Lynette;Zimmer, Jochen
Cellulose is frequently found in communities of sessile bacteria, called biofilms. E. coli and other enterobacteriaceae modify cellulose with phosphoethanolamine (pEtN) to promote host tissue adhesion. The E. coli pEtN cellulose biosynthesis machinery contains the catalytic BcsA-BcsB complex synthesizing and secreting cellulose, in addition to five other subunits. The membrane-anchored periplasmic BcsG subunit catalyzes pEtN modification. Here we present the cryo electron microscopy structure of the ~1 MDa E. coli Bcs complex, consisting of one BcsA enzyme associated with six copies of BcsB. BcsB homo-oligomerizes primarily through interactions of its carbohydrate-binding domains as well as intermolecular beta-sheet formation. The BcsB hexamer creates a half-spiral whose open side accommodates two BcsG subunits directly adjacent to BcsA’s periplasmic channel exit. The cytosolic BcsE and BcsQ subunits associate with BcsA’s regulatory PilZ-domain. The macrocomplex is a fascinating example of cellulose synthase specification.
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影响因子:
4.8
作者:
Anderson, Alexander C.;Burnett, Alysha J. N.;Weadge, Joel T.
通讯作者:
Weadge, Joel T.
影响因子:
14.9
作者:
Drozdetskiy A;Cole C;Procter J;Barton GJ
通讯作者:
Barton GJ
影响因子:
3.7
作者:
Du J;Vepachedu V;Cho SH;Kumar M;Nixon BT
通讯作者:
Nixon BT
影响因子:
6.4
作者:
Fan, Junping;Petersen, Erik M.;Miller, Samuel, I
通讯作者:
Miller, Samuel, I
DOI:
10.1073/pnas.1612927114
发表时间:
2017-02-28
影响因子:
11.1
作者:
Anandan, Anandhi;Evans, Genevieve L.;Vrielink, Alice
通讯作者:
Vrielink, Alice