Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form

Rhombohedral crystals of Mycobacterium tuberculosis phosphopantetheine adenylyltransferase

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Brown, K. L.
  • Morris, V. K.
  • Izard, T.

publication date

  • January 2004

journal

  • Acta Crystallographica Section D-Biological Crystallography  Journal

abstract

  • The penultimate step of prokaryotic coenzyme A (CoA) biosynthesis is directed by the essential enzyme phosphopantetheine adenylyltransferase (PPAT; EC 2.7.7.3), an attractive target for antibiotics. The reaction catalyzed by PPAT is rate-limiting and involves the transfer of an adenylyl group from ATP to 4'-phosphopantetheine to form 3'-dephospho-CoA. Rhombohedral crystals of PPAT from Mycobacterium tuberculosis (Rv2965c) were obtained. The crystals belong to space group R32, with unit-cell parameters a = 68.69 A, alpha = 91.81 degrees. The crystals diffract to better than 2 A resolution on a Cu Kalpha rotating-anode generator. The packing density for one polypeptide chain in the asymmetric unit is 2.89 A(3) Da(-1), with a solvent content of 0.57.

subject areas

  • Bacterial Proteins
  • Crystallization
  • Crystallography, X-Ray
  • Mycobacterium tuberculosis
  • Nucleotidyltransferases
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0907-4449

Digital Object Identifier (DOI)

  • 10.1107/s0907444903025988

PubMed ID

  • 14684928
scroll to property group menus

Additional Document Info

start page

  • 195

end page

  • 196

volume

  • 60

issue

  • Pt 1

©2021 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support