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Our studies suggest that the N\u2010terminal domain of ornithine decarboxylase folds into a \u03b2\/\u03b1\u2010barrel. Through the analysis of known barrel structures we developed a topographic model of the pyridoxal phosphate\u2010binding domain of ornithine decarboxylase, which predicts that the Schiff base lysine and a conserved glycine\u2010rich sequence both map to the C\u2010termini of the \u03b2\u2010strands. Other residues in this domain that are likely to have essential roles in catalysis, substrate, and cofactor binding were also identified, suggesting that this model will be a suitable guide to mutagenic analysis of the enzyme mechanism.<\/jats:p>","DOI":"10.1002\/pro.5560040705","type":"journal-article","created":{"date-parts":[[2009,2,10]],"date-time":"2009-02-10T02:47:21Z","timestamp":1234234041000},"page":"1291-1304","source":"Crossref","is-referenced-by-count":309,"title":["Modeling of the spatial structure of eukaryotic ornithine decarboxylases"],"prefix":"10.1002","volume":"4","author":[{"given":"Nick V.","family":"Grishin","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Margaret A.","family":"Phillips","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Elizabeth J.","family":"Goldsmith","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2008,12,31]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/0022-2836(87)90293-2"},{"key":"e_1_2_1_3_1","doi-asserted-by":"publisher","DOI":"10.1038\/2271098a0"},{"key":"e_1_2_1_4_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-1033.1994.tb18577.x"},{"key":"e_1_2_1_5_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00067a006"},{"key":"e_1_2_1_6_1","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/21.13.3097"},{"key":"e_1_2_1_7_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0022-2836(77)80200-3"},{"key":"e_1_2_1_8_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0959-440X(05)80118-6"},{"key":"e_1_2_1_9_1","doi-asserted-by":"publisher","DOI":"10.1002\/prot.340070307"},{"key":"e_1_2_1_10_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.1853201"},{"key":"e_1_2_1_11_1","doi-asserted-by":"publisher","DOI":"10.1002\/prot.340160110"},{"key":"e_1_2_1_12_1","doi-asserted-by":"publisher","DOI":"10.1002\/prot.340070202"},{"key":"e_1_2_1_13_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0959-440X(05)80114-9"},{"key":"e_1_2_1_14_1","doi-asserted-by":"publisher","DOI":"10.1016\/0968-0004(90)90035-A"},{"key":"e_1_2_1_15_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00399a066"},{"key":"e_1_2_1_16_1","volume-title":"Program manual for the GCG package, version 7, April 1991","author":"Genetics Computer Group.","year":"1991"},{"key":"e_1_2_1_17_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.84.13.4355"},{"key":"e_1_2_1_18_1","doi-asserted-by":"crossref","first-page":"17857","DOI":"10.1016\/S0021-9258(19)77913-7","article-title":"Three\u2010dimensional structure of the tryptophan synthase \u03b1\n                  2\n                  \u03b2\n                  2 multienzyme complex from","volume":"263","author":"Hyde CC","year":"1988","journal-title":"Salmonella typhimurium. 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