Preliminary crystallographic study of the Streptococcus agalactiae sortases, sortase A and sortase C1

Baldeep Khare; Alexandra Samal; Krishnan Vengadesan; K. R. Rajashankar; Xin Ma; I. Hsiu Huang; Hung Ton-That; Sthanam V.L. Narayana

doi:10.1107/S1744309110031106

Preliminary crystallographic study of the Streptococcus agalactiae sortases, sortase A and sortase C1

Baldeep Khare, Alexandra Samal, Krishnan Vengadesan, K. R. Rajashankar, Xin Ma, I. Hsiu Huang, Hung Ton-That, Sthanam V.L. Narayana

Biochemistry & Microbiology

Research output: Contribution to journal › Article › peer-review

8 Scopus citations

Abstract

Sortases are cysteine transpeptidases that are essential for the assembly and anchoring of cell-surface adhesins in Gram-positive bacteria. In Streptococcus agalactiae (GBS), the pilin-specific sortase SrtC1 catalyzes the polymerization of pilins encoded by pilus island 1 (PI-1) and the housekeeping sortase SrtA is necessary for cell-wall anchoring of the resulting pilus polymers. These sortases are known to utilize different substrates for pilus polymerization and cell-wall anchoring; however, the structural correlates that dictate their substrate specificity have not yet been clearly defined. This report presents the expression, purification and crystallization of SrtC1 (SAG0647) and SrtA (SAG0961) from S. agalactiae strain 2603V/R. The GBS SrtC1 has been crystallized in three crystal forms and the GBS SrtA has been crystallized in one crystal form.

Original language	English
Pages (from-to)	1096-1100
Number of pages	5
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	66
Issue number	9
DOIs	https://doi.org/10.1107/S1744309110031106
State	Published - 1 Sep 2010

Keywords

sortase A
sortase C1
sortases
Streptococcus agalactiae

Access to Document

10.1107/S1744309110031106

Cite this

Khare, B., Samal, A., Vengadesan, K., Rajashankar, K. R., Ma, X., Huang, I. H., Ton-That, H., & Narayana, S. V. L. (2010). Preliminary crystallographic study of the Streptococcus agalactiae sortases, sortase A and sortase C1. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 66(9), 1096-1100. https://doi.org/10.1107/S1744309110031106

@article{c011d9a0e1a145b8b94d705063b683e7,

title = "Preliminary crystallographic study of the Streptococcus agalactiae sortases, sortase A and sortase C1",

abstract = "Sortases are cysteine transpeptidases that are essential for the assembly and anchoring of cell-surface adhesins in Gram-positive bacteria. In Streptococcus agalactiae (GBS), the pilin-specific sortase SrtC1 catalyzes the polymerization of pilins encoded by pilus island 1 (PI-1) and the housekeeping sortase SrtA is necessary for cell-wall anchoring of the resulting pilus polymers. These sortases are known to utilize different substrates for pilus polymerization and cell-wall anchoring; however, the structural correlates that dictate their substrate specificity have not yet been clearly defined. This report presents the expression, purification and crystallization of SrtC1 (SAG0647) and SrtA (SAG0961) from S. agalactiae strain 2603V/R. The GBS SrtC1 has been crystallized in three crystal forms and the GBS SrtA has been crystallized in one crystal form.",

keywords = "sortase A, sortase C1, sortases, Streptococcus agalactiae",

author = "Baldeep Khare and Alexandra Samal and Krishnan Vengadesan and Rajashankar, {K. R.} and Xin Ma and Huang, {I. Hsiu} and Hung Ton-That and Narayana, {Sthanam V.L.}",

year = "2010",

month = sep,

day = "1",

doi = "10.1107/S1744309110031106",

language = "English",

volume = "66",

pages = "1096--1100",

journal = "Acta Crystallographica Section F: Structural Biology and Crystallization Communications",

issn = "1744-3091",

publisher = "Wiley-Blackwell Publishing Ltd",

number = "9",

}

Khare, B, Samal, A, Vengadesan, K, Rajashankar, KR, Ma, X, Huang, IH, Ton-That, H & Narayana, SVL 2010, 'Preliminary crystallographic study of the Streptococcus agalactiae sortases, sortase A and sortase C1', Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 66, no. 9, pp. 1096-1100. https://doi.org/10.1107/S1744309110031106

TY - JOUR

T1 - Preliminary crystallographic study of the Streptococcus agalactiae sortases, sortase A and sortase C1

AU - Khare, Baldeep

AU - Samal, Alexandra

AU - Vengadesan, Krishnan

AU - Rajashankar, K. R.

AU - Ma, Xin

AU - Huang, I. Hsiu

AU - Ton-That, Hung

AU - Narayana, Sthanam V.L.

PY - 2010/9/1

Y1 - 2010/9/1

N2 - Sortases are cysteine transpeptidases that are essential for the assembly and anchoring of cell-surface adhesins in Gram-positive bacteria. In Streptococcus agalactiae (GBS), the pilin-specific sortase SrtC1 catalyzes the polymerization of pilins encoded by pilus island 1 (PI-1) and the housekeeping sortase SrtA is necessary for cell-wall anchoring of the resulting pilus polymers. These sortases are known to utilize different substrates for pilus polymerization and cell-wall anchoring; however, the structural correlates that dictate their substrate specificity have not yet been clearly defined. This report presents the expression, purification and crystallization of SrtC1 (SAG0647) and SrtA (SAG0961) from S. agalactiae strain 2603V/R. The GBS SrtC1 has been crystallized in three crystal forms and the GBS SrtA has been crystallized in one crystal form.

AB - Sortases are cysteine transpeptidases that are essential for the assembly and anchoring of cell-surface adhesins in Gram-positive bacteria. In Streptococcus agalactiae (GBS), the pilin-specific sortase SrtC1 catalyzes the polymerization of pilins encoded by pilus island 1 (PI-1) and the housekeeping sortase SrtA is necessary for cell-wall anchoring of the resulting pilus polymers. These sortases are known to utilize different substrates for pilus polymerization and cell-wall anchoring; however, the structural correlates that dictate their substrate specificity have not yet been clearly defined. This report presents the expression, purification and crystallization of SrtC1 (SAG0647) and SrtA (SAG0961) from S. agalactiae strain 2603V/R. The GBS SrtC1 has been crystallized in three crystal forms and the GBS SrtA has been crystallized in one crystal form.

KW - sortase A

KW - sortase C1

KW - sortases

KW - Streptococcus agalactiae

UR - http://www.scopus.com/inward/record.url?scp=77956526569&partnerID=8YFLogxK

U2 - 10.1107/S1744309110031106

DO - 10.1107/S1744309110031106

M3 - Article

C2 - 20823536

AN - SCOPUS:77956526569

SN - 1744-3091

VL - 66

SP - 1096

EP - 1100

JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

IS - 9

ER -

Preliminary crystallographic study of the Streptococcus agalactiae sortases, sortase A and sortase C1

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this