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The last major review on this subject by Pabo &amp; Sauer (1984) summarized the structural and functional studies of the three sequence-specific DNA-binding proteins whose crystal structures were then known, the<jats:italic>E. coli<\/jats:italic>catabolite gene activator protein (CAP) (McKay &amp; Steitz, 1981; McKay<jats:italic>et al.<\/jats:italic>1982; Weber &amp; Steitz, 1987), a<jats:italic>cro<\/jats:italic>repressor from phage \u03bb (Anderson<jats:italic>et al.<\/jats:italic>1981), and the DNA-binding proteolytic fragment of<jats:italic>\u03bbcI<\/jats:italic>repressor protein (Pabo &amp; Lewis, 1982) Although crystallographic studies of the<jats:italic>E. coli lac<\/jats:italic>repressor protein were initiated as early as 1971 when it was the only regulatory protein available in sufficient quantities for structural studies (Steitz<jats:italic>et al.<\/jats:italic>1974), little was established about the structural aspects of DNA-binding proteins until the structure of CAP was determined in 1980 followed shortly thereafter by the structure of<jats:italic>\u03bbcro<\/jats:italic>repressor and subsequently that of the \u03bb repressor fragment. There are now determined at high resolution the crystal structures of seven prokaryotic gene regulatory proteins or fragments [CAP,<jats:italic>\u03bbcro<\/jats:italic>,<jats:italic>\u03bbcI<\/jats:italic>repressor fragment, 434 repressor fragment (Anderson<jats:italic>et al.<\/jats:italic>1987), 434<jats:italic>cro<\/jats:italic>repressor (Wolberger<jats:italic>et al.<\/jats:italic>1988),<jats:italic>E. coli trp<\/jats:italic>repressor (Schevitz<jats:italic>et al.<\/jats:italic>1985),<jats:italic>E. coli met<\/jats:italic>repressor (Rafferty<jats:italic>et al.<\/jats:italic>1989)],<jats:italic>EcoR<\/jats:italic>I restriction endonuclease (McClarin<jats:italic>et al.<\/jats:italic>1986), DNAse I (Suck &amp; Ofner, 1986), the catalytic domain of \u03b3\u03b4 resolvase (Hatfull<jats:italic>et al.<\/jats:italic>1989) and two sequence-independent double-stranded DNA-binding proteins [the Klenow fragment of<jats:italic>E. coli<\/jats:italic>DNA polymerase I (Ollis<jats:italic>et al.<\/jats:italic>1985) and the<jats:italic>E. coli<\/jats:italic>Hu protein (Tanaka<jats:italic>et al.<\/jats:italic>, 1984)].<\/jats:p>","DOI":"10.1017\/s0033583500005552","type":"journal-article","created":{"date-parts":[[2009,3,17]],"date-time":"2009-03-17T15:54:13Z","timestamp":1237305253000},"page":"205-280","source":"Crossref","is-referenced-by-count":413,"title":["Structural studies of protein\u2013nucleic acid interaction: the sources of sequence-specific binding"],"prefix":"10.1017","volume":"23","author":[{"given":"Thomas A.","family":"Steitz","sequence":"first","affiliation":[]}],"member":"56","published-online":{"date-parts":[[2009,3,17]]},"reference":[{"key":"S0033583500005552_ref199","doi-asserted-by":"publisher","DOI":"10.1016\/S0022-2836(59)80002-4"},{"key":"S0033583500005552_ref096","doi-asserted-by":"publisher","DOI":"10.1038\/322661a0"},{"key":"S0033583500005552_ref143","doi-asserted-by":"publisher","DOI":"10.1126\/science.2479982"},{"key":"S0033583500005552_ref095","unstructured":"Majors J. 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