HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

Cover Illustration: The three-dimensional structure of the protein AF2095 from the thermophilic archaea Archaeglobus fulgidis has been determined by NMR methods by the Northeast Structural Genomics Consortium (NESG). While the protein is of yet unknown biological function, the structural similarity between AF2095 and the human Pth2 protein suggests that the protein functions as a peptidyl-tRNA hydrolase. The AF2095 structure was also leveraged to obtain structural and functional information for 55 additional unannotated proteins found in eukaryotic, archaeal, and bacterial organisms, providing novel insights into the evolution of the Pth and Pth2 enzyme families. (See Powers et al., pp. 2849–2861.)