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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.

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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