{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,29]],"date-time":"2026-08-29T06:40:55Z","timestamp":1787985655562,"version":"build-2784847793"},"reference-count":21,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2009,11,24]],"date-time":"2009-11-24T00:00:00Z","timestamp":1259020800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Proteins"],"published-print":{"date-parts":[[2010,5]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>RG13 is a 72 kDa engineered allosteric enzyme comprised of a fusion between maltose binding protein (MBP) and TEM1 \u03b2\u2010lactamase (BLA) for which maltose is a positive effector of BLA activity. We have used NMR spectroscopy to acquire [<jats:sup>15<\/jats:sup>N, <jats:sup>1<\/jats:sup>H]\u2010TROSY\u2010HSQC spectra of RG13 in the presence and absence of maltose. The RG13 chemical shift data was compared to the published chemical shift data of MBP and BLA. The spectra are consistent with the expectation that the individual domain structures of RG13 are substantially conserved from MBP and BLA. Differences in the spectra are consistent with the fusion geometry of MBP and BLA and the maltose\u2010dependent differences in the kinetics of RG13 enzyme activity. In particular, the spectra provide evidence for a maltose\u2010dependent conformational change of a key active site glutamate involved in deacylation of the enzyme\u2010substrate intermediate. Proteins 2010. \u00a9 2009 Wiley\u2010Liss, Inc.<\/jats:p>","DOI":"10.1002\/prot.22657","type":"journal-article","created":{"date-parts":[[2009,11,24]],"date-time":"2009-11-24T19:39:28Z","timestamp":1259091568000},"page":"1423-1430","source":"Crossref","is-referenced-by-count":20,"title":["NMR characterization of an engineered domain fusion between maltose binding protein and TEM1 \u03b2\u2010lactamase provides insight into its structure and allosteric mechanism"],"prefix":"10.1002","volume":"78","author":[{"given":"Chapman M.","family":"Wright","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ananya","family":"Majumdar","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Joel R.","family":"Tolman","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marc","family":"Ostermeier","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2009,12,23]]},"reference":[{"key":"e_1_2_5_2_2","doi-asserted-by":"publisher","DOI":"10.1093\/protein\/gzi048"},{"key":"e_1_2_5_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.jmb.2003.12.016"},{"key":"e_1_2_5_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.chembiol.2004.08.020"},{"key":"e_1_2_5_5_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0502673102"},{"key":"e_1_2_5_6_2","doi-asserted-by":"crossref","first-page":"5327","DOI":"10.1016\/S0021-9258(17)42994-2","article-title":"Purification and properties of thiol beta\u2010lactamase. 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