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dc.contributor.authorMehboob, Shahila
dc.contributor.authorMulhearn, Debbie C.
dc.contributor.authorTruong, Kent
dc.contributor.authorJohnson, Michael E.
dc.contributor.authorSantarsiero, Bernard D.
dc.date.accessioned2011-05-27T18:41:26Z
dc.date.available2011-05-27T18:41:26Z
dc.date.issued2010-11
dc.identifier.bibliographicCitationMehboob, S., Mulhearn, D. C., Truong, K., Johnson, M. E., & Santarsiero, B. D. 2010. Structure of dihydroorotase from Bacillus anthracis at 2.6 A resolution. Acta Crystallographica Section F-Structural Biology and Crystallization Communications, 66: 1432-1435. DOI: 10.1107/S1744309110037085en
dc.identifier.issn1744-3091
dc.identifier.otherDOI: 10.1107/S1744309110037085
dc.identifier.urihttp://hdl.handle.net/10027/7775
dc.descriptionPost print version of article may differ from published version. The definitive version is available through International Union of Crystallography at DOI: 10.1107/S1744309110037085en
dc.description.abstractDihydroorotase (EC 3.5.2.3) catalyzes the reversible cyclization of N-carbamoyl-l-aspartate to l-dihydroorotate in the third step of the pyrimidine-biosynthesis pathway in Bacillus anthracis. A comparison is made between the structures of dihydroorotase from four different organisms, including B. anthracis dihydroorotase, and reveals substantial variations in the active site, dimer interface and overall tertiary structure. These differences demonstrate the utility of exploring multiple structures of a molecular target as expressed from different organisms and how these differences can be exploited for structure-based drug discovery.en
dc.description.sponsorshipNECAT Sector 24 is supported by the National Institutes of Health, National Center for Research Resources under grant No. RR-15301.en
dc.language.isoen_USen
dc.publisherInternational Union of Crystallographyen
dc.subjectdihydroorotatseen
dc.subjectBacillus anthracisen
dc.titleStructure of dihydroorotase from Bacillus anthracis at 2.6 A resolutionen
dc.typeArticleen


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