Tail tubular protein A: a dual-function tail protein of Klebsiella pneumoniae bacteriophage KP32

Abstract Tail tubular protein A (TTPA) is a structural tail protein of Klebsiella pneumoniae bacteriophage KP32, and is responsible for adhering the bacteriophage to host cells. For the first time, we found that TTPA also exhibits lytic activity towards capsular exopolysaccharide (EPS) of the multir...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Anna Pyra, Ewa Brzozowska, Krzysztof Pawlik, Andrzej Gamian, Miroslawa Dauter, Zbigniew Dauter
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/80dec92296cc4d7db087bd625c8d1c1d
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:80dec92296cc4d7db087bd625c8d1c1d
record_format	dspace
spelling	oai:doaj.org-article:80dec92296cc4d7db087bd625c8d1c1d2021-12-02T11:40:31ZTail tubular protein A: a dual-function tail protein of Klebsiella pneumoniae bacteriophage KP3210.1038/s41598-017-02451-32045-2322https://doaj.org/article/80dec92296cc4d7db087bd625c8d1c1d2017-05-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-02451-3https://doaj.org/toc/2045-2322Abstract Tail tubular protein A (TTPA) is a structural tail protein of Klebsiella pneumoniae bacteriophage KP32, and is responsible for adhering the bacteriophage to host cells. For the first time, we found that TTPA also exhibits lytic activity towards capsular exopolysaccharide (EPS) of the multiresistant clinical strain of Klebsiella pneumoniae, PCM2713, and thus should be regarded as a dual-function macromolecule that exhibits both structural and enzymatic actions. Here, we present our crystallographic and enzymatic studies of TTPA. TTPA was crystallized and X-ray diffraction data were collected to a resolution of 1.9 Å. In the crystal, TTPA molecules were found to adopt a tetrameric structure with α-helical domains on one side and β-strands and loops on the other. The novel crystal structure of TTPA resembles those of the bacteriophage T7 tail protein gp11 and gp4 of bacteriophage P22, but TTPA contains an additional antiparallel β-sheet carrying a lectin-like domain that could be responsible for EPS binding. The enzymatic activity of TTPA may reflect the presence of a peptidoglycan hydrolase domain in the α-helical region (amino acid residues 126 to 173). These novel results provide new insights into the enzymatic mechanism through which TTPA acts on polysaccharides.Anna PyraEwa BrzozowskaKrzysztof PawlikAndrzej GamianMiroslawa DauterZbigniew DauterNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-9 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Anna Pyra Ewa Brzozowska Krzysztof Pawlik Andrzej Gamian Miroslawa Dauter Zbigniew Dauter Tail tubular protein A: a dual-function tail protein of Klebsiella pneumoniae bacteriophage KP32
description	Abstract Tail tubular protein A (TTPA) is a structural tail protein of Klebsiella pneumoniae bacteriophage KP32, and is responsible for adhering the bacteriophage to host cells. For the first time, we found that TTPA also exhibits lytic activity towards capsular exopolysaccharide (EPS) of the multiresistant clinical strain of Klebsiella pneumoniae, PCM2713, and thus should be regarded as a dual-function macromolecule that exhibits both structural and enzymatic actions. Here, we present our crystallographic and enzymatic studies of TTPA. TTPA was crystallized and X-ray diffraction data were collected to a resolution of 1.9 Å. In the crystal, TTPA molecules were found to adopt a tetrameric structure with α-helical domains on one side and β-strands and loops on the other. The novel crystal structure of TTPA resembles those of the bacteriophage T7 tail protein gp11 and gp4 of bacteriophage P22, but TTPA contains an additional antiparallel β-sheet carrying a lectin-like domain that could be responsible for EPS binding. The enzymatic activity of TTPA may reflect the presence of a peptidoglycan hydrolase domain in the α-helical region (amino acid residues 126 to 173). These novel results provide new insights into the enzymatic mechanism through which TTPA acts on polysaccharides.
format	article
author	Anna Pyra Ewa Brzozowska Krzysztof Pawlik Andrzej Gamian Miroslawa Dauter Zbigniew Dauter
author_facet	Anna Pyra Ewa Brzozowska Krzysztof Pawlik Andrzej Gamian Miroslawa Dauter Zbigniew Dauter
author_sort	Anna Pyra
title	Tail tubular protein A: a dual-function tail protein of Klebsiella pneumoniae bacteriophage KP32
title_short	Tail tubular protein A: a dual-function tail protein of Klebsiella pneumoniae bacteriophage KP32
title_full	Tail tubular protein A: a dual-function tail protein of Klebsiella pneumoniae bacteriophage KP32
title_fullStr	Tail tubular protein A: a dual-function tail protein of Klebsiella pneumoniae bacteriophage KP32
title_full_unstemmed	Tail tubular protein A: a dual-function tail protein of Klebsiella pneumoniae bacteriophage KP32
title_sort	tail tubular protein a: a dual-function tail protein of klebsiella pneumoniae bacteriophage kp32
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/80dec92296cc4d7db087bd625c8d1c1d
work_keys_str_mv	AT annapyra tailtubularproteinaadualfunctiontailproteinofklebsiellapneumoniaebacteriophagekp32 AT ewabrzozowska tailtubularproteinaadualfunctiontailproteinofklebsiellapneumoniaebacteriophagekp32 AT krzysztofpawlik tailtubularproteinaadualfunctiontailproteinofklebsiellapneumoniaebacteriophagekp32 AT andrzejgamian tailtubularproteinaadualfunctiontailproteinofklebsiellapneumoniaebacteriophagekp32 AT miroslawadauter tailtubularproteinaadualfunctiontailproteinofklebsiellapneumoniaebacteriophagekp32 AT zbigniewdauter tailtubularproteinaadualfunctiontailproteinofklebsiellapneumoniaebacteriophagekp32
_version_	1718395591755563008

Tail tubular protein A: a dual-function tail protein of Klebsiella pneumoniae bacteriophage KP32

Ejemplares similares