Structure of the 3.3 MDa, in vitro assembled, hubless
bacteriophage T4 baseplate

J 2014

Structure of the 3.3 MDa, in vitro assembled, hubless bacteriophage T4 baseplate

YAP, Moh Lan, Thomas KLOSE, Pavel PLEVKA, Anastasia AKSYUK, Xinzheng ZHANG et. al.

Základní údaje

Originální název

Structure of the 3.3 MDa, in vitro assembled, hubless bacteriophage T4 baseplate

Autoři

YAP, Moh Lan, Thomas KLOSE, Pavel PLEVKA, Anastasia AKSYUK, Xinzheng ZHANG, Fumio ARISAKA a Michael G. ROSSMANN

Vydání

Journal of Structural Biology, UNITED STATES, ACADEMIC PRESS INC ELSEVIER SCIENCE, 2014, 1047-8477

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Impakt faktor

Impact factor: 3.231

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1016/j.jsb.2014.06.008

UT WoS

000340217300001

Klíčová slova anglicky

Bacteriophage T4; Baseplate; X-ray crystallography; Low resolution

Štítky

neMU

Změněno: 29. 3. 2017 10:58, Mgr. Eva Špillingová

Anotace

V originále

The bacteriophage T4 baseplate is the control center of the virus, where the recognition of an Escherichia coli host by the long tail fibers is translated into a signal to initiate infection. The short tail fibers unfold from the baseplate for firm attachment to the host, followed by shrinkage of the tail sheath that causes the tail tube to enter and cross the periplasmic space ending with injection of the genome into the host. During this process, the 6.5 MDa baseplate changes its structure from a "dome" shape to a "star" shape. An in vitro assembled hubless baseplate has been crystallized. It consists of six copies of the recombinantly expressed trimeric gene product (gp) 10, monomeric gp7, dimeric gp8, dimeric gp6 and monomeric gp53. The diffraction pattern extends, at most, to 4.0 angstrom resolution. The known partial structures of gp10, gp8, and gp6 and their relative position in the baseplate derived from earlier electron microscopy studies were used for molecular replacement. An electron density map has been calculated based on molecular replacement, single isomorphous replacement with anomalous dispersion data and 2-fold non-crystallographic symmetry averaging between two baseplate wedges in the crystallographic asymmetric unit. The current electron density map indicates that there are structural changes in the gp6, gp8, and gp10 oligomers compared to their structures when separately crystallized. Additional density is also visible corresponding to gp7, gp53 and the unknown parts of gp10 and gp6. (C) 2014 Elsevier Inc. All rights reserved.

Citovat

YAP, Moh Lan, Thomas KLOSE, Pavel PLEVKA, Anastasia AKSYUK, Xinzheng ZHANG, Fumio ARISAKA a Michael G. ROSSMANN. Structure of the 3.3 MDa, in vitro assembled, hubless bacteriophage T4 baseplate. Journal of Structural Biology. UNITED STATES: ACADEMIC PRESS INC ELSEVIER SCIENCE, 2014, roč. 187, č. 2, s. 95-102. ISSN 1047-8477. Dostupné z: https://dx.doi.org/10.1016/j.jsb.2014.06.008.

@article{1376791,
   author = {Yap, Moh Lan and Klose, Thomas and Plevka, Pavel and Aksyuk, Anastasia and Zhang, Xinzheng and Arisaka, Fumio and Rossmann, Michael G.},
   article_location = {UNITED STATES},
   article_number = {2},
   doi = {http://dx.doi.org/10.1016/j.jsb.2014.06.008},
   keywords = {Bacteriophage T4; Baseplate; X-ray crystallography; Low resolution},
   language = {eng},
   issn = {1047-8477},
   journal = {Journal of Structural Biology},
   title = {Structure of the 3.3 MDa, in vitro assembled, hubless bacteriophage T4 baseplate},
   volume = {187},
   year = {2014}
}

TY  - JOUR
ID  - 1376791
AU  - Yap, Moh Lan - Klose, Thomas - Plevka, Pavel - Aksyuk, Anastasia - Zhang, Xinzheng - Arisaka, Fumio - Rossmann, Michael G.
PY  - 2014
TI  - Structure of the 3.3 MDa, in vitro assembled, hubless bacteriophage T4 baseplate
JF  - Journal of Structural Biology
VL  - 187
IS  - 2
SP  - 95-102
EP  - 95-102
PB  - ACADEMIC PRESS INC ELSEVIER SCIENCE
SN  - 10478477
KW  - Bacteriophage T4
KW  - Baseplate
KW  - X-ray crystallography
KW  - Low resolution
N2  - The bacteriophage T4 baseplate is the control center of the virus, where the recognition of an Escherichia coli host by the long tail fibers is translated into a signal to initiate infection. The short tail fibers unfold from the baseplate for firm attachment to the host, followed by shrinkage of the tail sheath that causes the tail tube to enter and cross the periplasmic space ending with injection of the genome into the host. During this process, the 6.5 MDa baseplate changes its structure from a "dome" shape to a "star" shape. An in vitro assembled hubless baseplate has been crystallized. It consists of six copies of the recombinantly expressed trimeric gene product (gp) 10, monomeric gp7, dimeric gp8, dimeric gp6 and monomeric gp53. The diffraction pattern extends, at most, to 4.0 angstrom resolution. The known partial structures of gp10, gp8, and gp6 and their relative position in the baseplate derived from earlier electron microscopy studies were used for molecular replacement. An electron density map has been calculated based on molecular replacement, single isomorphous replacement with anomalous dispersion data and 2-fold non-crystallographic symmetry averaging between two baseplate wedges in the crystallographic asymmetric unit. The current electron density map indicates that there are structural changes in the gp6, gp8, and gp10 oligomers compared to their structures when separately crystallized. Additional density is also visible corresponding to gp7, gp53 and the unknown parts of gp10 and gp6. (C) 2014 Elsevier Inc. All rights reserved.
ER  -

YAP, Moh Lan, Thomas KLOSE, Pavel PLEVKA, Anastasia AKSYUK, Xinzheng ZHANG, Fumio ARISAKA a Michael G. ROSSMANN. Structure of the 3.3 MDa, in vitro assembled, hubless bacteriophage T4 baseplate. \textit{Journal of Structural Biology}. UNITED STATES: ACADEMIC PRESS INC ELSEVIER SCIENCE, 2014, roč.~187, č.~2, s.~95-102. ISSN~1047-8477. Dostupné z: https://dx.doi.org/10.1016/j.jsb.2014.06.008.

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