Deciphering the catalytic domain of colicin M, a peptidoglycan lipid II-degrading enzyme. - Wikidata - wikimedia - TriplyDB

Deciphering the catalytic domain of colicin M, a peptidoglycan lipid II-degrading enzyme.

Deciphering the catalytic domain of colicin M, a peptidoglycan lipid II-degrading enzyme.

http://www.wikidata.org/entity/Q38346419

about

Beware of proteins bearing gifts: protein antibiotics that use iron as a Trojan horse X-Ray Structure and Site-Directed Mutagenesis Analysis of the Escherichia coli Colicin M Immunity Protein Activation of Colicin M by the FkpA Prolyl Cis-Trans Isomerase/Chaperone Functional and Structural Characterization of PaeM, a Colicin M-like Bacteriocin Produced by Pseudomonas aeruginosa The Crystal Structure of the Lipid II-degrading Bacteriocin Syringacin M Suggests Unexpected Evolutionary Relationships between Colicin M-like Bacteriocins Structure of the atypical bacteriocin pectocin M2 implies a novel mechanism of protein uptake Mapping functional domains of colicin M.Bacterial cell wall. MurJ is the flippase of lipid-linked precursors for peptidoglycan biogenesis.Ferredoxin containing bacteriocins suggest a novel mechanism of iron uptake in Pectobacterium spp Global transcriptional responses to the bacteriocin colicin M in Escherichia coli.Distinct colicin M-like bacteriocin-immunity pairs in Burkholderia.Pectocin M1 (PcaM1) Inhibits Escherichia coli Cell Growth and Peptidoglycan Biosynthesis through Periplasmic Expression A Natural Chimeric Pseudomonas Bacteriocin with Novel Pore-Forming Activity Parasitizes the Ferrichrome Transporter.Nuclease colicins and their immunity proteins.Translocation trumps receptor binding in colicin entry into Escherichia coli.Structure and uptake mechanism of bacteriocins targeting peptidoglycan renewal.Toxicity of the colicin M catalytic domain exported to the periplasm is FkpA independent.CbrA is a flavin adenine dinucleotide protein that modifies the Escherichia coli outer membrane and confers specific resistance to Colicin M Plant-expressed pyocins for control of Pseudomonas aeruginosa.Colicin M, a peptidoglycan lipid-II-degrading enzyme: potential use for antibacterial means?The ColM Family, Polymorphic Toxins Breaching the Bacterial Cell Wall.Import of periplasmic bacteriocins targeting the murein.Lipid II-Degrading M-Class Bacteriocins A Colicin M-Type Bacteriocin from Pseudomonas aeruginosa Targeting the HxuC Heme Receptor Requires a Novel Immunity Partner

P2860

Q26863492-AA03F183-CA86-4A49-896B-558C9D996555 Q27665474-E7297925-D9D6-4E64-A01D-64E48E9951C8 Q27666344-0B6BD58F-3036-4DAA-A0D7-D3B3F9B67B44 Q27673139-33AFC37C-37C9-4551-89FE-E22DD954E0CD Q27673487-4CACA923-01A5-479D-BC9E-DF480D4A7BFB Q27683962-B57C98AE-EAE5-4AAB-9204-7E90BE4A69DE Q30155927-7CE6BE72-F3B6-4801-89B5-1E7745B9700A Q34175962-2BE6444A-1BD3-4520-B1B2-7E7403C311ED Q34200327-0E89C625-E1AE-476A-A8C7-51C8AAEB4736 Q34591603-772371B2-7149-4972-A873-A5F1F327930A Q36323901-75560D86-CD7F-443B-9689-63ED686CA01A Q37533577-48AA243D-C0A0-4016-8BE0-BBE96E73726E Q37712113-63C28FBE-A6C8-4E32-AAF7-79FA715451BB Q37956420-75E79206-531E-4A90-A841-8A6EC0639576 Q38061999-30FD44BA-D5C0-4919-89D6-EAEA627A3C67 Q41405708-90F8872F-BFF3-4051-AB11-215B106890A7 Q41837430-5AAA0626-2776-46BC-83BC-A6E68891FDE2 Q42321821-AE548319-0030-45CE-8FB1-032E03E08F35 Q42369619-16E349E7-85E3-4B52-A56F-D3DCCB27B873 Q42677915-455212D8-0627-4202-8149-72516CE2ECC1 Q50026012-E138FC30-C36E-4F02-A1D2-3EEDF5102616 Q50774279-CCC59A39-5543-44BF-A277-5F32E1A9288D Q57836033-B17CB721-56A5-4D8A-8958-B3F5E5FD0EBA Q58022977-A2548939-A1B6-44BC-8544-67D2E10C773F

P2860

Deciphering the catalytic domain of colicin M, a peptidoglycan lipid II-degrading enzyme.

http://www.wikidata.org/entity/Q38346419

description

2010 nî lūn-bûn

@nan

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

2010年论文

@zh

2010年论文

@zh-cn

name

Deciphering the catalytic domain of colicin M, a peptidoglycan lipid II-degrading enzyme.

@en

type

label

Deciphering the catalytic domain of colicin M, a peptidoglycan lipid II-degrading enzyme.

@en

prefLabel

Deciphering the catalytic domain of colicin M, a peptidoglycan lipid II-degrading enzyme.

@en

P1433

Q38346419-77525235-EF08-485C-A998-F8494EFED1DD

P1476

Q38346419-97926EC1-D0F4-4C5C-A42A-88F8703351FC

P2093

Q38346419-58ACF533-41AD-4E0A-855C-AC86C6E46A41

Q38346419-5C77F7E9-E353-49DE-8003-8F4369F2950F

Q38346419-60ACE2EC-E346-4603-BA70-123B6DA04D56

Q38346419-830CAC76-183A-41C9-8D56-6DF6DF8CB230

Q38346419-9CE9904C-0E3E-439D-B4E5-E84A16962AD1

Q38346419-B4D5669B-3A04-4B76-A8F0-1ABB39CE85C2

Q38346419-BB7841FE-A11C-48BF-89EC-DFCA2D6FBAE2

P2860

Q38346419-04865CFA-2CCC-4507-BBB7-87025A33D41E

Q38346419-0704AAB6-6AD1-490D-B1F9-1A449850E415

Q38346419-0757483F-CD78-49BA-B3CD-9B4EF18FB829

Q38346419-0CBCB013-52F6-4B1D-B56C-F657F0ED1E17

Q38346419-1197EAAB-BF6B-4995-AA20-8C29121757C4

Q38346419-123C4A39-7860-4DB1-9F5C-A726C429C88D

Q38346419-1613FCEC-37D3-4D3F-AF07-B261A363B07C

Q38346419-1BF06DA8-8D6E-44A3-90B8-3D00AF894802

Q38346419-1F05AA1C-9CCE-4D67-A9B7-D2F3C829DD69

Q38346419-362506E4-8679-4F77-B5A1-23E663AD4707

P304

Q38346419-D6837DF3-3A45-4651-AAFC-83201BB0D40E

P31

Q38346419-9C8479DB-8FFF-466E-BCE9-8EF2E92935B8

P356

Q38346419-0769E13F-6147-4E61-8F84-E8A2DEB91F0F

P407

Q38346419-38F93053-C885-4DAE-A652-F9D0B5BF6153

P433

Q38346419-2C9910EC-64C2-4F9D-9E56-57F8B9AD16A8

P478

Q38346419-66EAEB47-74E3-4560-9263-FEF82D8C81AC

P50

Q38346419-06952522-C9EC-450E-92CE-1055AA493B02

Q38346419-1F5B130F-8167-48A9-946E-6B7F577B18CC

Q38346419-89B40947-8B93-4393-9CAD-9D916A09C927

P577

Q38346419-65B228BD-789B-4F93-8452-41B868618581

P698

Q38346419-3B441DB9-ACD3-43BF-9304-06082D2A3F0A

P932

Q38346419-060A61C7-33E9-4A97-8DBD-14117A46F0C7

P356

JBC.M109.093583

P1433

Journal of Biological Chemistry

P1476

Deciphering the catalytic domain of colicin M, a peptidoglycan lipid II-degrading enzyme.

@en

P2093

Ahmed Bouhss

http://www.w3.org/2001/XMLSchema#string

Boubekeur Boussaid

http://www.w3.org/2001/XMLSchema#string

Denis Duché

http://www.w3.org/2001/XMLSchema#string

Didier Blanot

http://www.w3.org/2001/XMLSchema#string

Fabien Gérard

http://www.w3.org/2001/XMLSchema#string

Hélène Barreteau

http://www.w3.org/2001/XMLSchema#string

Roland Lloubès

http://www.w3.org/2001/XMLSchema#string

P2860

Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection

Colicin biology

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity

Crystal Structure of Colicin M, a Novel Phosphatase Specifically Imported by Escherichia coli>

The structure and mechanism of protein phosphatases: insights into catalysis and regulation

Peptidoglycan structure and architecture

Import of biopolymers into Escherichia coli: nucleotide sequences of the exbB and exbD genes are homologous to those of the tolQ and tolR genes, respectively.

Human- and plant-pathogenic Pseudomonas species produce bacteriocins exhibiting colicin M-like hydrolase activity towards peptidoglycan precursors

Prolonged incubation in calcium chloride improves the competence of Escherichia coli cells.

P304

12378-12389

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1074/JBC.M109.093583

http://www.w3.org/2001/XMLSchema#string

P407

P433

16

http://www.w3.org/2001/XMLSchema#string

P478

285

http://www.w3.org/2001/XMLSchema#string

P50

Dominique Mengin-Lecreulx

P577

2010-02-16T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

20159977

http://www.w3.org/2001/XMLSchema#string

P932

2852976

http://www.w3.org/2001/XMLSchema#string