Related ArticlesNMR assignments for the insertion domain of bacteriophage CUS-3 coat protein.
Biomol NMR Assign. 2015 Feb 19;
Authors: Tripler TN, Maciejewski MW, Teschke CM, Alexandrescu AT
Abstract
CUS-3 is a P22-like tailed dsDNA bacteriophage that infects Escherichia coli serotype K1. The CUS-3 coat protein, which forms the icosahedral capsid, has a conserved HK97-fold but with a non-conserved accessory domain known as the insertion domain (I-domain). Sequence alignment of the coat proteins from CUS-3 and P22 shows higher sequence similarity for the I-domains (35*%) than for the HK97-cores, suggesting the I-domains play important functional roles. The I-domain of the P22 coat protein, which has an NMR structure comprised of a six-stranded ?-barrel, has been shown to govern the assembly, stability and size of the resulting capsid particles. Here, we report the (1)H, (15)N, and (13)C assignments for the I-domain from the coat protein of bacteriophage CUS-3. The secondary structure and dynamics of the CUS-3 I-domain, predicted from the assigned NMR chemical shifts, agree with those of the P22 I-domain, suggesting the CUS-3 and P22 I-domains may have similar structures and functions in capsid assembly.
PMID: 25694158 [PubMed - as supplied by publisher]
[NMR paper] Multiple Functional Roles of the Accessory I-Domain of Bacteriophage P22 Coat Protein Revealed by NMR Structure and CryoEM Modeling.
Multiple Functional Roles of the Accessory I-Domain of Bacteriophage P22 Coat Protein Revealed by NMR Structure and CryoEM Modeling.
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Structure. 2014 May 14;
Authors: Rizzo AA, Suhanovsky MM, Baker ML, Fraser LC, Jones LM, Rempel DL, Gross ML, Chiu W, Alexandrescu AT, Teschke CM
Abstract
Some capsid proteins built on the ubiquitous HK97-fold have accessory domains imparting specific...
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Multiple Functional Roles of the Accessory I-Domain of Bacteriophage P22 Coat Protein Revealed by NMR Structure and CryoEM Modeling
Multiple Functional Roles of the Accessory I-Domain of Bacteriophage P22 Coat Protein Revealed by NMR Structure and CryoEM Modeling
Publication date: Available online 15 May 2014
Source:Structure</br>
Author(s): Alessandro*A. Rizzo , Margaret*M. Suhanovsky , Matthew*L. Baker , LaTasha*C.R. Fraser , Lisa*M. Jones , Don*L. Rempel , Michael*L. Gross , Wah Chiu , Andrei*T. Alexandrescu , Carolyn*M. Teschke</br>
Some capsid proteins built on the ubiquitous HK97-fold have accessory domains imparting specific functions. Bacteriophage P22 coat protein has a unique...
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05-15-2014 07:23 PM
[NMR paper] Structure of the coat protein in Pf1 bacteriophage determined by solid-state NMR spec
Structure of the coat protein in Pf1 bacteriophage determined by solid-state NMR spectroscopy.
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J Mol Biol. 2004 Aug 13;341(3):869-79
Authors: Thiriot DS, Nevzorov AA, Zagyanskiy L, Wu CH, Opella SJ
The atomic resolution structure of Pf1 coat protein determined by solid-state NMR spectroscopy of magnetically aligned filamentous bacteriophage particles in solution is compared to the structures previously determined by X-ray fiber and...
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[NMR paper] Structure of the coat protein in fd filamentous bacteriophage particles determined by
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Proc Natl Acad Sci U S A. 2003 May 27;100(11):6458-63
Authors: Zeri AC, Mesleh MF, Nevzorov AA, Opella SJ
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Science. 1991 May 31;252(5010):1303-5
Authors: Shon KJ, Kim Y, Colnago LA, Opella SJ
Filamentous bacteriophage coat protein undergoes a remarkable structural transition during the viral assembly process as it is transferred from the membrane environment of the cell, where it spans the phospholipid bilayer, to the newly extruded virus particles....
NMR assignments for the insertion domain of bacteriophage CUS-3 coat protein.
Linear Mode
