3U80

1.60 Angstrom Resolution Crystal Structure of a 3-Dehydroquinate Dehydratase-like Protein from Bifidobacterium longum

Summary for 3U80

• Entry DOI: 10.2210/pdb3u80/pdb
• Descriptor: 3-dehydroquinate dehydratase, type II (2 entities in total)
• Functional Keywords: structural genomics, center for structural genomics of infectious diseases, csgid, unknown function
• Biological source: Bifidobacterium longum
• Total number of polymer chains: 2
• Total formula weight: 33494.08

Authors

Light, S.H.,Minasov, G.,Shuvalova, L.,Papazisi, L.,Lavie, A.,Anderson, W.F.,Center for Structural Genomics of Infectious Diseases (CSGID) (deposition date: 2011-10-14, release date: 2011-10-26, Last modification date: 2023-09-13)

Primary citation

Light, S.H.,Krishna, S.N.,Bergan, R.C.,Lavie, A.,Anderson, W.F.
Crystal structure of a type II dehydroquinate dehydratase-like protein from Bifidobacterium longum.
J.Struct.Funct.Genom., 14:25-30, 2013

PubMed 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.

PubMed: 23539270
DOI: 10.1007/s10969-013-9149-7

Experimental method

X-RAY DIFFRACTION (1.6 Å)