High-resolution crystal structure of MltE, an outer membrane-anchored endolytic peptidoglycan lytic transglycosylase from Escherichia coli.

High-resolution crystal structure of MltE, an outer membrane-anchored endolytic peptidoglycan lytic transglycosylase from Escherichia coli.
复制标题

DOI:
10.1021/bi200085y
复制
发表时间:
2011-04-05
期刊:
影响因子:
2.9
通讯作者:
Hermoso JA
Hermoso JA
中科院分区:
生物学3区
文献类型:
--
作者:
Artola-Recolons C;Carrasco-López C;Llarrull LI;Kumarasiri M;Lastochkin E;Martínez de Ilarduya I;Meindl K;Usón I;Mobashery S;Hermoso JA

文献摘要

参考文献

被引文献

相似文献

本文报道了大肠杆菌中第一个内溶肽聚糖裂解转糖基化酶MltE的晶体结构。这种酶的降解活性启动了细胞壁再循环的过程,这是细菌生存中不可或缺的事件。该结构揭示了MltE如何识别其底物——细胞壁肽聚糖。这也解释了这种内溶酶在肽聚糖链中间切割的能力。此外,该结构揭示了酶是如何被隔离在外膜的内叶上的。
The crystal structure of the first endolytic peptidoglycan lytic transglycosylase MltE from Escherichia coli is reported herein. The degradative activity of this enzyme initiates the process of cell wall recycling, which is an integral event in the bacterial existence. The structure sheds light on how MltE recognizes its substrate, the cell wall peptidoglycan. It also explains the ability of this endolytic enzyme to cleave in the middle of the peptidoglycan chains. Furthermore, the structure reveals how the enzyme is sequestered on the inner leaf let of the outer membrane.
DOI: 10.1128/jb.180.13.3441-3447.1998
发表时间: 1998-07-01
影响因子: 3.2
作者:
Kraft, AR;Templin, MF;Höltje, JV
通讯作者: Höltje, JV
DOI: 10.1038/367750a0
发表时间: 1994-02-24
期刊: NATURE
影响因子: 64.8
作者:
THUNNISSEN, AMWH;DIJKSTRA, AJ;DIJKSTRA, BW
通讯作者: DIJKSTRA, BW
DOI: 10.1111/j.1432-1033.1981.tb05342.x
发表时间: 1981-01-01
期刊: EUROPEAN JOURNAL OF BIOCHEMISTRY
影响因子: --
作者:
BEACHEY, EH;KECK, W;SCHWARZ, U
通讯作者: SCHWARZ, U
DOI: 10.1038/nmeth.1365
发表时间: 2009-09-01
期刊: NATURE METHODS
影响因子: 48
作者:
Rodriguez, Dayte D.;Grosse, Christian;Uson, Isabel
通讯作者: Uson, Isabel
DOI: 10.1074/jbc.m701818200
发表时间: 2007-07-20
影响因子: 4.8
作者:
van Straaten, Karin E.;Barends, Thomas R. M.;Thunnissen, Andy-Mark W. H.
通讯作者: Thunnissen, Andy-Mark W. H.