The PE-PPE domain in mycobacterium reveals a serine α/β hydrolase fold and function: an in-silico analysis.

The PE and PPE proteins first reported in the genome sequence of Mycobacterium tuberculosis strain H37Rv are now identified in all mycobacterial species. The PE-PPE domain (Pfam ID: PF08237) is a 225 amino acid residue conserved region located towards the C-terminus of some PE and PPE proteins and h...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Rafiya Sultana, Karunakar Tanneeru, Lalitha Guruprasad
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/95d6ff943f064bc2a587cf9103a78b1b
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:95d6ff943f064bc2a587cf9103a78b1b
record_format	dspace
spelling	oai:doaj.org-article:95d6ff943f064bc2a587cf9103a78b1b2021-11-18T06:58:59ZThe PE-PPE domain in mycobacterium reveals a serine α/β hydrolase fold and function: an in-silico analysis.1932-620310.1371/journal.pone.0016745https://doaj.org/article/95d6ff943f064bc2a587cf9103a78b1b2011-02-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21347309/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203The PE and PPE proteins first reported in the genome sequence of Mycobacterium tuberculosis strain H37Rv are now identified in all mycobacterial species. The PE-PPE domain (Pfam ID: PF08237) is a 225 amino acid residue conserved region located towards the C-terminus of some PE and PPE proteins and hypothetical proteins. Our in-silico sequence analysis revealed that this domain is present in all Mycobacteria, some Rhodococcus and Nocardia farcinica genomes. This domain comprises a pentapeptide sequence motif GxSxG/S at the N-terminus and conserved amino acid residues Ser, Asp and His that constitute a catalytic triad characteristic of lipase, esterase and cutinase activity. The fold prediction and comparative modeling of the 3-D structure of the PE-PPE domain revealed a "serine α/β hydrolase" structure with a central β-sheet flanked by α-helices on either side. The structure comprises a lid insertion with a closed structure conformation and has a solvent inaccessible active site. The oxyanion hole that stabilizes the negative charge on the tetrahedral intermediate has been identified. Our findings add to the growing list of serine hydrolases in mycobacterium, which are essential for the maintenance of their impermeable cell wall and virulence. These results provide the directions for the design of experiments to establish the function of PE and PPE proteins.Rafiya SultanaKarunakar TanneeruLalitha GuruprasadPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 2, p e16745 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Rafiya Sultana Karunakar Tanneeru Lalitha Guruprasad The PE-PPE domain in mycobacterium reveals a serine α/β hydrolase fold and function: an in-silico analysis.
description	The PE and PPE proteins first reported in the genome sequence of Mycobacterium tuberculosis strain H37Rv are now identified in all mycobacterial species. The PE-PPE domain (Pfam ID: PF08237) is a 225 amino acid residue conserved region located towards the C-terminus of some PE and PPE proteins and hypothetical proteins. Our in-silico sequence analysis revealed that this domain is present in all Mycobacteria, some Rhodococcus and Nocardia farcinica genomes. This domain comprises a pentapeptide sequence motif GxSxG/S at the N-terminus and conserved amino acid residues Ser, Asp and His that constitute a catalytic triad characteristic of lipase, esterase and cutinase activity. The fold prediction and comparative modeling of the 3-D structure of the PE-PPE domain revealed a "serine α/β hydrolase" structure with a central β-sheet flanked by α-helices on either side. The structure comprises a lid insertion with a closed structure conformation and has a solvent inaccessible active site. The oxyanion hole that stabilizes the negative charge on the tetrahedral intermediate has been identified. Our findings add to the growing list of serine hydrolases in mycobacterium, which are essential for the maintenance of their impermeable cell wall and virulence. These results provide the directions for the design of experiments to establish the function of PE and PPE proteins.
format	article
author	Rafiya Sultana Karunakar Tanneeru Lalitha Guruprasad
author_facet	Rafiya Sultana Karunakar Tanneeru Lalitha Guruprasad
author_sort	Rafiya Sultana
title	The PE-PPE domain in mycobacterium reveals a serine α/β hydrolase fold and function: an in-silico analysis.
title_short	The PE-PPE domain in mycobacterium reveals a serine α/β hydrolase fold and function: an in-silico analysis.
title_full	The PE-PPE domain in mycobacterium reveals a serine α/β hydrolase fold and function: an in-silico analysis.
title_fullStr	The PE-PPE domain in mycobacterium reveals a serine α/β hydrolase fold and function: an in-silico analysis.
title_full_unstemmed	The PE-PPE domain in mycobacterium reveals a serine α/β hydrolase fold and function: an in-silico analysis.
title_sort	pe-ppe domain in mycobacterium reveals a serine α/β hydrolase fold and function: an in-silico analysis.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/95d6ff943f064bc2a587cf9103a78b1b
work_keys_str_mv	AT rafiyasultana thepeppedomaininmycobacteriumrevealsaserineabhydrolasefoldandfunctionaninsilicoanalysis AT karunakartanneeru thepeppedomaininmycobacteriumrevealsaserineabhydrolasefoldandfunctionaninsilicoanalysis AT lalithaguruprasad thepeppedomaininmycobacteriumrevealsaserineabhydrolasefoldandfunctionaninsilicoanalysis AT rafiyasultana peppedomaininmycobacteriumrevealsaserineabhydrolasefoldandfunctionaninsilicoanalysis AT karunakartanneeru peppedomaininmycobacteriumrevealsaserineabhydrolasefoldandfunctionaninsilicoanalysis AT lalithaguruprasad peppedomaininmycobacteriumrevealsaserineabhydrolasefoldandfunctionaninsilicoanalysis
_version_	1718424119239770112

The PE-PPE domain in mycobacterium reveals a serine α/β hydrolase fold and function: an in-silico analysis.

Ejemplares similares