Structural highlights
Function
[D6ZTY6_BIFLJ] Catalyzes a trans-dehydration via an enolate intermediate (By similarity).[HAMAP-Rule:MF_00169]
Publication Abstract from PubMed
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.
Crystal structure of a type II dehydroquinate dehydratase-like protein from Bifidobacterium longum.,Light SH, Krishna SN, Bergan RC, Lavie A, Anderson WF J Struct Funct Genomics. 2013 Mar;14(1):25-30. doi: 10.1007/s10969-013-9149-7., Epub 2013 Mar 29. PMID:23539270[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Light SH, Krishna SN, Bergan RC, Lavie A, Anderson WF. Crystal structure of a type II dehydroquinate dehydratase-like protein from Bifidobacterium longum. J Struct Funct Genomics. 2013 Mar;14(1):25-30. doi: 10.1007/s10969-013-9149-7., Epub 2013 Mar 29. PMID:23539270 doi:http://dx.doi.org/10.1007/s10969-013-9149-7
