We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

5mf2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 12: Line 12:
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
-
The tail of Caudovirales bacteriophages serves as an adsorption device, a host cell wall-perforating machine and a genome delivery pathway. In Siphoviridae, the assembly of the long and flexible tail is a highly cooperative and regulated process that is initiated from the proteins forming the distal tail tip complex. In Gram-positive infecting siphophages, the Distal tail (Dit) protein has been structurally characterised, and is proposed to represent a baseplate hub docking structure. It is organised as a hexameric ring that connects the tail tube and the adsorption device. In this study we report the characterisation of pb9, a tail tip protein of Escherichia coli bacteriophage T5. By immunolocalisation we show that pb9 is located in the upper cone of T5 tail tip, at the end of the tail tube. The crystal structure of pb9 reveals a two-domain protein. Domain A exhibits remarkable structural similarity with the N-terminal domain of known Dit proteins, while domain B adopts an Oligosaccharide/oligonucleotide Binding-fold (OB-fold) that is not shared by these proteins. We thus propose that pb9 is the Dit protein of T5, making it the first Dit protein described for a Gram-negative infecting siphophages. Multiple sequence alignments suggest that pb9 is a paradigm for a large family of Dit proteins of siphopages infecting mostly gram-negative hosts. The modular structure of the Dit protein maintains the basic building block that would be conserved among all siphophages, combining it with a more divergent domain that might serve specific host adhesion properties.
+
Macromolecular crystallography suffers from two major issues: getting well-diffracting crystals and solving the phase problem inherent to large macromolecules. Here, we describe the first example of a lanthanide complex family named "crystallophore" (Xo4), which contributes to tackling both bottlenecks. This terbium complex, Tb-Xo4, is an appealing agent for biocrystallography, combining the exceptional phasing power of the Tb(iii) heavy atom with powerful nucleating properties, providing ready-to-use crystals for structure determination. Furthermore, protein/Tb-Xo4 co-crystals can be easily detected and discriminated from other crystalline by-products using luminescence. We demonstrate the potential of this additive for the crystallisation and structure determination of eight proteins, two of whose structures were unknown.
-
Crystal structure of pb9, the distal tail protein of bacteriophage T5: A conserved structural motif among all siphophages.,Flayhan A, Vellieux FM, Lurz R, Maury O, Contreras-Martel C, Girard E, Boulanger P, Breyton C J Virol. 2013 Oct 23. PMID:24155371<ref>PMID:24155371</ref>
+
Crystallophore: a versatile lanthanide complex for protein crystallography combining nucleating effects, phasing properties, and luminescence.,Engilberge S, Riobe F, Di Pietro S, Lassalle L, Coquelle N, Arnaud CA, Pitrat D, Mulatier JC, Madern D, Breyton C, Maury O, Girard E Chem Sci. 2017 Sep 1;8(9):5909-5917. doi: 10.1039/c7sc00758b. Epub 2017 Jun 6. PMID:29619195<ref>PMID:29619195</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

Revision as of 06:25, 18 April 2018

Bacteriophage T5 distal tail protein pb9 co-crystallized with Tb-Xo4

5mf2, resolution 2.00Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5mf2"
Personal tools