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

@inproceedings{Xu2010StructureOA,
  title={Structure of an essential bacterial protein YeaZ (TM0874) from Thermotoga maritima at 2.5 {\AA} resolution},
  author={Qingping Xu and Daniel McMullan and Lukasz Jaroszewski and S. Sri Krishna and Marc-Andr{\'e} Elsliger and Andrew P. Yeh and Polat Abdubek and Tamara Astakhova and Herbert L. Axelrod and Dennis W. Carlton and H L Chiu and Thomas Clayton and Lian Duan and Julie Feuerhelm and Joanna C. Grant and Gye Won Han and Kevin Kai Jin and Heath E. Klock and Mark W. Knuth and Mitchell D Miller and Andrew T. Morse and Edward Nigoghossian and Linda Okach and Silvya Oommachen and Jessica Paulsen and Ron Reyes and Christopher L. Rife and Henry van den Bedem and Keith O Hodgson and John Wooley and Ashley Deacon and Adam Godzik and Scott A. Lesley and Ian A. Wilson},
  booktitle={Acta crystallographica. Section F, Structural biology and crystallization communications},
  year={2010}
}
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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