{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,16]],"date-time":"2026-06-16T09:23:37Z","timestamp":1781601817652,"version":"3.54.5"},"reference-count":63,"publisher":"Springer Science and Business Media LLC","issue":"1","content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["BMC Struct Biol"],"published-print":{"date-parts":[[2009,12]]},"abstract":"<jats:title>Abstract<\/jats:title>\n          <jats:sec>\n            <jats:title>Background<\/jats:title>\n            <jats:p>\n              <jats:italic>Bacillus anthracis<\/jats:italic> is the causative agent of anthrax and a potential bioterrorism threat. Here we report the biochemical and structural characterization of <jats:italic>B. anthracis<\/jats:italic> (Ames) alanine racemase (Alr<jats:sub>\n                <jats:italic>Bax<\/jats:italic>\n              <\/jats:sub>), an essential enzyme in prokaryotes and a target for antimicrobial drug development. We also compare the native Alr<jats:sub>\n                <jats:italic>Bax<\/jats:italic>\n              <\/jats:sub>structure to a recently reported structure of the same enzyme obtained through reductive lysine methylation.<\/jats:p>\n          <\/jats:sec>\n          <jats:sec>\n            <jats:title>Results<\/jats:title>\n            <jats:p>\n              <jats:italic>B. anthracis<\/jats:italic> has two open reading frames encoding for putative alanine racemases. We show that only one, <jats:italic>dal1<\/jats:italic>, is able to complement a D-alanine auxotrophic strain of <jats:italic>E. coli<\/jats:italic>. Purified Dal1, which we term Alr<jats:sub>\n                <jats:italic>Bax<\/jats:italic>\n              <\/jats:sub>, is shown to be a dimer in solution by dynamic light scattering and has a V<jats:sub>max<\/jats:sub> for racemization (L- to D-alanine) of 101 U\/mg. The crystal structure of unmodified Alr<jats:sub>\n                <jats:italic>Bax<\/jats:italic>\n              <\/jats:sub>is reported here to 1.95 \u00c5 resolution. Despite the overall similarity of the fold to other alanine racemases, Alr<jats:sub>\n                <jats:italic>Bax<\/jats:italic>\n              <\/jats:sub>makes use of a chloride ion to position key active site residues for catalysis, a feature not yet observed for this enzyme in other species. Crystal contacts are more extensive in the methylated structure compared to the unmethylated structure.<\/jats:p>\n          <\/jats:sec>\n          <jats:sec>\n            <jats:title>Conclusion<\/jats:title>\n            <jats:p>The chloride ion in Alr<jats:sub>\n                <jats:italic>Bax<\/jats:italic>\n              <\/jats:sub>is functioning effectively as a carbamylated lysine making it an integral and unique part of this structure. Despite differences in space group and crystal form, the two Alr<jats:sub>\n                <jats:italic>Bax<\/jats:italic>\n              <\/jats:sub>structures are very similar, supporting the case that reductive methylation is a valid rescue strategy for proteins recalcitrant to crystallization, and does not, in this case, result in artifacts in the tertiary structure.<\/jats:p>\n          <\/jats:sec>","DOI":"10.1186\/1472-6807-9-53","type":"journal-article","created":{"date-parts":[[2009,8,20]],"date-time":"2009-08-20T18:14:14Z","timestamp":1250792054000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":28,"title":["Biochemical and structural characterization of alanine racemase from Bacillus anthracis (Ames)"],"prefix":"10.1186","volume":"9","author":[{"given":"Rafael M","family":"Cou\u00f1ago","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Milya","family":"Davlieva","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ulrich","family":"Strych","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ryan E","family":"Hill","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kurt L","family":"Krause","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2009,8,20]]},"reference":[{"issue":"11","key":"273_CR1","doi-asserted-by":"publisher","first-page":"815","DOI":"10.1056\/NEJM199909093411107","volume":"341","author":"TC Dixon","year":"1999","unstructured":"Dixon TC, Meselson M, Guillemin J, Hanna PC: Anthrax. 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