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Structure of an essential bacterial protein YeaZ (TM0874) from Thermotoga maritima at 2.5 Å resolution
- 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.
Published Web Location
https://doi.org/10.1107/s1744309109022192Abstract
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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