Ontology highlight
ABSTRACT:
SUBMITTER: Xu Q
PROVIDER: S-EPMC2954210 | biostudies-literature | 2010 Oct
REPOSITORIES: biostudies-literature
Xu Qingping Q McMullan Daniel D Jaroszewski Lukasz L Krishna S Sri SS Elsliger Marc André MA Yeh Andrew P AP Abdubek Polat P Astakhova Tamara T Axelrod Herbert L HL Carlton Dennis D Chiu Hsiu Ju HJ Clayton Thomas T Duan Lian L Feuerhelm Julie J Grant Joanna J Han Gye Won GW Jin Kevin K KK Klock Heath E HE Knuth Mark W MW Miller Mitchell D MD Morse Andrew T AT Nigoghossian Edward E Okach Linda L Oommachen Silvya S Paulsen Jessica J Reyes Ron R Rife Christopher L CL van den Bedem Henry H Hodgson Keith O KO Wooley John J Deacon Ashley M AM Godzik Adam A Lesley Scott A SA Wilson Ian A IA
Acta crystallographica. Section F, Structural biology and crystallization communications 20091027 Pt 10
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. ...[more]