2max: Difference between revisions

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'''Unreleased structure'''
{{STRUCTURE_2max|  PDB=2max  |  SCENE=  }}
===NMR structure of the RNA polymerase alpha subunit C-terminal domain from Helicobacter pylori===
{{ABSTRACT_PUBMED_24442709}}


The entry 2max is ON HOLD  until Paper Publication
==Function==
[[http://www.uniprot.org/uniprot/RPOA_HELPJ RPOA_HELPJ]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (By similarity).


Authors: Borin, B.N., Krezel, A.M.
==About this Structure==
[[2max]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MAX OCA].  


Description: NMR structure of the RNA polymerase alpha subunit C-terminal domain from Helicobacter pylori
==Reference==
<ref group="xtra">PMID:024442709</ref><references group="xtra"/><references/>
[[Category: DNA-directed RNA polymerase]]
[[Category: Borin, B N.]]
[[Category: Krezel, A M.]]
[[Category: Dna-directed rna polymerase]]
[[Category: Hp1293]]
[[Category: Jhp1213]]
[[Category: Nucleotidyltransferase]]
[[Category: Rna polymerase alpha subunit]]
[[Category: Rpoa]]
[[Category: Transcription]]
[[Category: Transferase]]

Revision as of 16:33, 12 March 2014

Template:STRUCTURE 2max

NMR structure of the RNA polymerase alpha subunit C-terminal domain from Helicobacter pyloriNMR structure of the RNA polymerase alpha subunit C-terminal domain from Helicobacter pylori

Template:ABSTRACT PUBMED 24442709

FunctionFunction

[RPOA_HELPJ] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (By similarity).

About this StructureAbout this Structure

2max is a 1 chain structure. Full experimental information is available from OCA.

ReferenceReference

[xtra 1]

  1. Borin BN, Tang W, Krezel AM. Helicobacter pylori RNA polymerase alpha-subunit C-terminal domain shows features unique to varepsilon-proteobacteria and binds NikR/DNA complexes. Protein Sci. 2014 Jan 17. doi: 10.1002/pro.2427. PMID:24442709 doi:http://dx.doi.org/10.1002/pro.2427

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