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Crystal structure of a type II dehydroquinate dehydratase-like protein from Bifidobacterium longum |
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| Authors: | Samuel H. Light Sankar N. Krishna Raymond C. Bergan Arnon Lavie Wayne F. Anderson |
| Affiliation: | 1. Center for Structural Genomics of Infectious Diseases and Department of Molecular Pharmacology and Biological Chemistry, Feinberg School of Medicine, Northwestern University, Chicago, IL, 60611, USA 2. Department of Medicine, Robert H. Lurie Cancer Center, Center for Molecular Innovation and Drug Discovery, Feinberg School of Medicine, Northwestern University, Chicago, IL, 60611, USA 3. Department of Biochemistry and Molecular Genetics, University of Illinois at Chicago, Chicago, IL, 60607, USA |
| Abstract: | Dehydroquinate dehydratase (DHQD) catalyzes the third step in the biosynthetic shikimate pathway. Here we identify a Bifidobacterium longum protein with high sequence homology to type II DHQDs but no detectable DHQD activity under standard assay conditions. A crystal structure reveals that the B. longum protein adopts a DHQD-like tertiary structure but a distinct quaternary state. Apparently forming a dimer, the B. longum protein lacks the active site aspartic acid contributed from a neighboring protomer in the type II DHQD dodecamer. Relating to the absence of protein–protein interactions established in the type II DHQD dodecameric assembly, substantial conformational changes distinguish the would-be active site of the B. longum protein. As B. longum possess no other genes with homology to known DHQDs, these findings imply a unique DHQD activity within B. longum. |
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