NMR structural study of N-terminal domain of RNA polymerase
delta subunit from Bacillus subtilis

a 2009

NMR structural study of N-terminal domain of RNA polymerase delta subunit from Bacillus subtilis

MOTÁČKOVÁ, Veronika, Hana ŠANDEROVÁ, Jiří NOVÁČEK, Lukáš ŽÍDEK, Libor KRÁSNÝ et. al.

Základní údaje

Originální název

NMR structural study of N-terminal domain of RNA polymerase delta subunit from Bacillus subtilis

Název česky

NMR strukturní studie N-terminální domény delta podjednotky RNA polymerasy z Bacilla subtila

Autoři

MOTÁČKOVÁ, Veronika, Hana ŠANDEROVÁ, Jiří NOVÁČEK, Lukáš ŽÍDEK, Libor KRÁSNÝ a Vladimír SKLENÁŘ

Vydání

VII Discussions in Structural Molecular Biology Nové Hrady, 2009

Další údaje

Typ výsledku

Konferenční abstrakt

Utajení

není předmětem státního či obchodního tajemství

Organizační jednotka

Přírodovědecká fakulta

ISSN

Klíčová slova anglicky

nmr; RNA polymerase; delta subunit; assignment; structure

Štítky

assignment, delta subunit, NMR, RNA polymerase, structure

Příznaky

Mezinárodní význam

Změněno: 4. 5. 2009 10:00, Mgr. Veronika Papoušková, Ph.D.

Anotace

V originále

Contrary to the well studied RNA polymerases of gram negative bacteria, RNA polymerase of Bacillus subtilis, a gram positive bacterium, contains two additional subunits, referred to as delta and omega1. A well-structured N-terminal domain of subunit delta has been overexpressed in an E. coli expression system, labeled with stable isotopes C-13 and N-15, and investigated by nuclear magnetic resonance. A standard set of triple resonance NMR experiments was measured and almost all resonances of the protein backbone were assigned. Resonance frequencies of the side-chains were assigned using 3D TOCSY- and NOESY-type spectra. Three-bond coupling constant J(HNHA) were obtained from 3D HNHA experiments. Chemical shifts of backbone nuclei, medium range NOEs, and the three-bond coupling constants were analyzed and secondary structure was predicted. Internuclear distance restraints were extracted from NOESY spectra and used in structure calculation.

Návaznosti

GA204/09/0583, projekt VaV

Název: Delta podjednotka RNA polymerázy z Gram pozitivních bakterií (Akronym: DELTA)

Investor: Grantová agentura ČR, Delta podjednotka RNA polymerázy z Gram pozitivních bakterií

LC06030, projekt VaV

Název: Biomolekulární centrum

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Biomolekulární centrum

MSM0021622413, záměr

Název: Proteiny v metabolismu a při interakci organismů s prostředím

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Proteiny v metabolismu a při interakci organismů s prostředím

Citovat

MOTÁČKOVÁ, Veronika, Hana ŠANDEROVÁ, Jiří NOVÁČEK, Lukáš ŽÍDEK, Libor KRÁSNÝ a Vladimír SKLENÁŘ. NMR structural study of N-terminal domain of RNA polymerase delta subunit from Bacillus subtilis. In VII Discussions in Structural Molecular Biology Nové Hrady. 2009. ISSN 1211-5894.

@proceedings{830572,
   author = {Motáčková, Veronika and Šanderová, Hana and Nováček, Jiří and Žídek, Lukáš and Krásný, Libor and Sklenář, Vladimír},
   booktitle = {VII Discussions in Structural Molecular Biology Nové Hrady},
   keywords = {nmr; RNA polymerase; delta subunit; assignment; structure},
   title = {NMR structural study of N-terminal domain of RNA polymerase delta subunit from Bacillus subtilis},
   year = {2009}
}

TY  - CONF
ID  - 830572
AU  - Motáčková, Veronika - Šanderová, Hana - Nováček, Jiří - Žídek, Lukáš - Krásný, Libor - Sklenář, Vladimír
PY  - 2009
TI  - NMR structural study of N-terminal domain of RNA polymerase delta subunit from Bacillus subtilis
KW  - nmr
KW  - RNA polymerase
KW  - delta subunit
KW  - assignment
KW  - structure
N2  - Contrary to the well studied RNA polymerases of gram negative bacteria, RNA polymerase of Bacillus subtilis, a gram positive bacterium, contains two additional subunits, referred to as delta and omega1. A well-structured N-terminal domain of subunit delta has been overexpressed in an E. coli expression system, labeled with stable isotopes C-13 and N-15, and investigated by nuclear magnetic resonance. A standard set of triple resonance NMR experiments was measured and almost all resonances of the protein backbone were assigned. Resonance frequencies of the side-chains were assigned using 3D TOCSY- and NOESY-type spectra. Three-bond coupling constant J(HNHA) were obtained from 3D HNHA experiments. Chemical shifts of backbone nuclei, medium range NOEs, and the three-bond coupling constants were analyzed and secondary structure was predicted. Internuclear distance restraints were extracted from NOESY spectra and used in structure calculation.
ER  -

MOTÁČKOVÁ, Veronika, Hana ŠANDEROVÁ, Jiří NOVÁČEK, Lukáš ŽÍDEK, Libor KRÁSNÝ a Vladimír SKLENÁŘ. NMR structural study of N-terminal domain of RNA polymerase delta subunit from Bacillus subtilis. In \textit{VII Discussions in Structural Molecular Biology Nové Hrady}. 2009. ISSN~1211-5894.

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