Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:1.6
Classification:UNKNOWN FUNCTION
Release Date:2011-10-26
Deposition Date:2011-10-14
Revision Date:2013-05-08#2017-11-08
Molecular Weight:33494.08
Macromolecule Type:Protein
Residue Count:302
Atom Site Count:2068
DOI:10.2210/pdb3u80/pdb
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.
Resolution:1.6
Classification:UNKNOWN FUNCTION
Release Date:2011-10-26
Deposition Date:2011-10-14
Revision Date:2013-05-08#2017-11-08
Molecular Weight:33494.08
Macromolecule Type:Protein
Residue Count:302
Atom Site Count:2068
DOI:10.2210/pdb3u80/pdb
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.
| Date made available | 2011 |
|---|---|
| Publisher | RCSB-PDB |