Crystal structure of the anthrax lethal factor
dc.contributor.author | Pannifer, A. D. | en_US |
dc.contributor.author | Wong, Thiang Yian | en_US |
dc.contributor.author | Schwarzenbacher, R. | en_US |
dc.contributor.author | Renatus, M. | en_US |
dc.contributor.author | Petosa, C. | en_US |
dc.contributor.author | Bienkowska, J. | en_US |
dc.contributor.author | Lacy, D. B. | en_US |
dc.contributor.author | Collier, R. John | en_US |
dc.contributor.author | Park, Sukjoon | en_US |
dc.contributor.author | Leppla, S. H. | en_US |
dc.contributor.author | Hanna, Philip C. | en_US |
dc.contributor.author | Liddington, R. C. | en_US |
dc.date.accessioned | 2009-06-01T17:36:37Z | |
dc.date.available | 2009-06-01T17:36:37Z | |
dc.date.issued | 2001-11-08 | en_US |
dc.identifier.citation | Pannifer, AD; Wong, TY; Schwarzenbacher, R; Renatus, M; Petosa, C; Bienkowska, J; Lacy, DB; Collier, RJ; Park, S; Leppla, SH; Hanna, P; Liddington, RC. (2001) "Crystal structure of the anthrax lethal factor." Nature 414(6860): 229-233. <http://hdl.handle.net/2027.42/62772> | en_US |
dc.identifier.issn | 0028-0836 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/62772 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=11700563&dopt=citation | en_US |
dc.description.abstract | Lethal factor (LF) is a protein (relative molecular mass 90,000) that is critical in the pathogenesis of anthrax(1-3). It is a highly specific protease that cleaves members of the mitogen-activated protein kinase kinase (MAPKK) family near to their amino termini, leading to the inhibition of one or more signalling pathways(4-6). Here we describe the crystal structure of LF and its complex with the N terminus of MAPKK-2. LF comprises four domains: domain I binds the membrane-translocating component of anthrax toxin, the protective antigen (PA); domains II, III and IV together create a long deep groove that holds the 16-residue N-terminal tail of MAPKK-2 before cleavage. Domain II resembles the ADP-ribosylating toxin from Bacillus cereus, but the active site has been mutated and recruited to augment substrate recognition. Domain III is inserted into domain II, and seems to have arisen from a repeated duplication of a structural element of domain II. Domain IV is distantly related to the zinc metalloprotease family, and contains the catalytic centre; it also resembles domain I. The structure thus reveals a protein that has evolved through a process of gene duplication, mutation and fusion, into an enzyme with high and unusual specificity. | en_US |
dc.format.extent | 322166 bytes | |
dc.format.extent | 2489 bytes | |
dc.format.mimetype | application/octet-stream | |
dc.format.mimetype | text/plain | |
dc.publisher | Macmillan Publishers Ltd. | en_US |
dc.source | Nature | en_US |
dc.title | Crystal structure of the anthrax lethal factor | en_US |
dc.type | Article | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Univ Michigan, Sch Med, Dept Microbiol & Immunol, Ann Arbor, MI 48109 USA | en_US |
dc.contributor.affiliationother | Burnham Inst, La Jolla, CA 92037 USA | en_US |
dc.contributor.affiliationother | Univ Leicester, Dept Biochem, Leicester LE1 7RH, Leics, England | en_US |
dc.contributor.affiliationother | Dana Farber Canc Inst, Boston, MA 02115 USA | en_US |
dc.contributor.affiliationother | Harvard Univ, Sch Med, Dept Microbiol & Mol Genet, Boston, MA 02115 USA | en_US |
dc.contributor.affiliationother | Natl Inst Dent & Craniofacial Res, NIH, Bethesda, MD 20892 USA | en_US |
dc.identifier.pmid | 11700563 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/62772/1/414229a0.pdf | |
dc.identifier.doi | http://dx.doi.org/10.1038/n35101998 | en_US |
dc.identifier.source | Nature | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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