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Structure of an essential bacterial protein YeaZ (TM0874) from Thermotoga maritima at 2.5 Å resolution.

  • Author(s): Xu, Qingping
  • McMullan, Daniel
  • Jaroszewski, Lukasz
  • Krishna, S Sri
  • Elsliger, Marc André
  • Yeh, Andrew P
  • Abdubek, Polat
  • Astakhova, Tamara
  • Axelrod, Herbert L
  • Carlton, Dennis
  • Chiu, Hsiu Ju
  • Clayton, Thomas
  • Duan, Lian
  • Feuerhelm, Julie
  • Grant, Joanna
  • Han, Gye Won
  • Jin, Kevin K
  • Klock, Heath E
  • Knuth, Mark W
  • Miller, Mitchell D
  • Morse, Andrew T
  • Nigoghossian, Edward
  • Okach, Linda
  • Oommachen, Silvya
  • Paulsen, Jessica
  • Reyes, Ron
  • Rife, Christopher L
  • van den Bedem, Henry
  • Hodgson, Keith O
  • Wooley, John
  • Deacon, Ashley M
  • Godzik, Adam
  • Lesley, Scott A
  • Wilson, Ian A
  • et al.
Abstract

YeaZ is involved in a protein network that is essential for bacteria. The crystal structure of YeaZ from Thermotoga maritima was determined to 2.5 Å resolution. Although this protein belongs to a family of ancient actin-like ATPases, it appears that it has lost the ability to bind ATP since it lacks some key structural features that are important for interaction with ATP. A conserved surface was identified, supporting its role in the formation of protein complexes.

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