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Second-site suppression studies performed with a number of the primary mutants revealed a tight packing arrangement between spans I and II that is important for function and an additional interaction between spans I and III. We also postulate that a third motif, GXXIG, present in span I and highly conserved within different members of the amino acid-polyamine-organocation family, may function as a dimerization motif. Surprisingly, other highly conserved residues, such as Y60 and L41, could be replaced by various residues with no apparent loss of activity.<\/jats:p>","DOI":"10.1128\/jb.185.21.6225-6232.2003","type":"journal-article","created":{"date-parts":[[2003,10,15]],"date-time":"2003-10-15T19:52:45Z","timestamp":1066247565000},"page":"6225-6232","update-policy":"http:\/\/dx.doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":11,"title":["Putative Interhelical Interactions within the PheP Protein Revealed by Second-Site Suppressor Analysis"],"prefix":"10.1128","volume":"185","author":[{"given":"C.","family":"Dogovski","sequence":"first","affiliation":[{"name":"Department of Microbiology and Immunology, The University of Melbourne, Victoria 3010, Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"J.","family":"Pi","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology, The University of Melbourne, Victoria 3010, Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"A. 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