Comparison of four different crystal forms of the Mycobacterium tuberculosis ESX-1 secreted protein regulator EspR

Shanti Gangwar, Sita R. Meena, Ajay K. Saxena

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

The Mycobacterium tuberculosis ESX-1 secreted protein regulator (EspR, Rv3849) is the key protein that delivers bacterial proteins into the host cell during mycobacterial infection. EspR binds directly to the espACD operon and is involved in transcriptional activation. In the current study, M. tuberculosis EspR has been crystallized and its X-ray structure has been determined at 3.3 Å resolution in a P3221 crystal form. EspR forms a physiological dimer in the crystal. Each EspR monomer contains an N-terminal helix-turn-helix DNA-binding domain and a C-terminal dimerization domain. The EspR structure in the P3221 crystal form was compared with previously determined EspR structures in P32, P21 and P212121 crystal forms. Structural comparison analysis indicated that the N-terminal helix-turn-helix domain of EspR acquires a rigid structure in the four crystal forms. However, significant structural differences were observed in the C-terminal domain of EspR in the P21 crystal form when compared with the P3221 and P32 crystal forms. The interaction, stabilization energy and buried surface area analysis of EspR in the four different crystal forms have provided information about the physiological dimer interface of EspR.

Original languageEnglish (US)
Pages (from-to)433-437
Number of pages5
JournalActa Crystallographica Section F:Structural Biology Communications
Volume70
Issue number4
DOIs
StatePublished - 2014
Externally publishedYes

Fingerprint

tuberculosis
regulators
Mycobacterium tuberculosis
proteins
Crystals
Bacterial Proteins
Dimerization
Operon
helices
Transcriptional Activation
crystals
Proteins
X-Rays
DNA
Infection
Dimers
dimers
Rigid structures
infectious diseases
rigid structures

Keywords

  • M. tuberculosis EspR

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Genetics
  • Structural Biology
  • Condensed Matter Physics
  • Medicine(all)

Cite this

Comparison of four different crystal forms of the Mycobacterium tuberculosis ESX-1 secreted protein regulator EspR. / Gangwar, Shanti; Meena, Sita R.; Saxena, Ajay K.

In: Acta Crystallographica Section F:Structural Biology Communications, Vol. 70, No. 4, 2014, p. 433-437.

Research output: Contribution to journalArticle

@article{cc70f321763b4b7bb66207d4cfb01209,
title = "Comparison of four different crystal forms of the Mycobacterium tuberculosis ESX-1 secreted protein regulator EspR",
abstract = "The Mycobacterium tuberculosis ESX-1 secreted protein regulator (EspR, Rv3849) is the key protein that delivers bacterial proteins into the host cell during mycobacterial infection. EspR binds directly to the espACD operon and is involved in transcriptional activation. In the current study, M. tuberculosis EspR has been crystallized and its X-ray structure has been determined at 3.3 {\AA} resolution in a P3221 crystal form. EspR forms a physiological dimer in the crystal. Each EspR monomer contains an N-terminal helix-turn-helix DNA-binding domain and a C-terminal dimerization domain. The EspR structure in the P3221 crystal form was compared with previously determined EspR structures in P32, P21 and P212121 crystal forms. Structural comparison analysis indicated that the N-terminal helix-turn-helix domain of EspR acquires a rigid structure in the four crystal forms. However, significant structural differences were observed in the C-terminal domain of EspR in the P21 crystal form when compared with the P3221 and P32 crystal forms. The interaction, stabilization energy and buried surface area analysis of EspR in the four different crystal forms have provided information about the physiological dimer interface of EspR.",
keywords = "M. tuberculosis EspR",
author = "Shanti Gangwar and Meena, {Sita R.} and Saxena, {Ajay K.}",
year = "2014",
doi = "10.1107/S2053230X14004166",
language = "English (US)",
volume = "70",
pages = "433--437",
journal = "Acta Crystallographica Section F:Structural Biology Communications",
issn = "1744-3091",
publisher = "John Wiley and Sons Ltd",
number = "4",

}

TY - JOUR

T1 - Comparison of four different crystal forms of the Mycobacterium tuberculosis ESX-1 secreted protein regulator EspR

AU - Gangwar, Shanti

AU - Meena, Sita R.

AU - Saxena, Ajay K.

PY - 2014

Y1 - 2014

N2 - The Mycobacterium tuberculosis ESX-1 secreted protein regulator (EspR, Rv3849) is the key protein that delivers bacterial proteins into the host cell during mycobacterial infection. EspR binds directly to the espACD operon and is involved in transcriptional activation. In the current study, M. tuberculosis EspR has been crystallized and its X-ray structure has been determined at 3.3 Å resolution in a P3221 crystal form. EspR forms a physiological dimer in the crystal. Each EspR monomer contains an N-terminal helix-turn-helix DNA-binding domain and a C-terminal dimerization domain. The EspR structure in the P3221 crystal form was compared with previously determined EspR structures in P32, P21 and P212121 crystal forms. Structural comparison analysis indicated that the N-terminal helix-turn-helix domain of EspR acquires a rigid structure in the four crystal forms. However, significant structural differences were observed in the C-terminal domain of EspR in the P21 crystal form when compared with the P3221 and P32 crystal forms. The interaction, stabilization energy and buried surface area analysis of EspR in the four different crystal forms have provided information about the physiological dimer interface of EspR.

AB - The Mycobacterium tuberculosis ESX-1 secreted protein regulator (EspR, Rv3849) is the key protein that delivers bacterial proteins into the host cell during mycobacterial infection. EspR binds directly to the espACD operon and is involved in transcriptional activation. In the current study, M. tuberculosis EspR has been crystallized and its X-ray structure has been determined at 3.3 Å resolution in a P3221 crystal form. EspR forms a physiological dimer in the crystal. Each EspR monomer contains an N-terminal helix-turn-helix DNA-binding domain and a C-terminal dimerization domain. The EspR structure in the P3221 crystal form was compared with previously determined EspR structures in P32, P21 and P212121 crystal forms. Structural comparison analysis indicated that the N-terminal helix-turn-helix domain of EspR acquires a rigid structure in the four crystal forms. However, significant structural differences were observed in the C-terminal domain of EspR in the P21 crystal form when compared with the P3221 and P32 crystal forms. The interaction, stabilization energy and buried surface area analysis of EspR in the four different crystal forms have provided information about the physiological dimer interface of EspR.

KW - M. tuberculosis EspR

UR - http://www.scopus.com/inward/record.url?scp=84905436015&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84905436015&partnerID=8YFLogxK

U2 - 10.1107/S2053230X14004166

DO - 10.1107/S2053230X14004166

M3 - Article

C2 - 24699733

AN - SCOPUS:84905436015

VL - 70

SP - 433

EP - 437

JO - Acta Crystallographica Section F:Structural Biology Communications

JF - Acta Crystallographica Section F:Structural Biology Communications

SN - 1744-3091

IS - 4

ER -