| Title | Crystal structure of putative transcriptional regulator containing a LuxR DNA binding domain (NP_811094.1) from Bacteroides thetaiotaomicron VPI-5482 at 2.04 A resolution. To be published | | Site | JCSG | | PDB Id | | Target Id | 383272 | | Molecular Characteristics | | Source | Bacteroides thetaiotaomicron vpi-5482 | | Alias Ids | TPS1770,NP_811094.1 | Molecular Weight | 29573.30 Da. | | Residues | 257 | Isoelectric Point | 5.87 | | Sequence | mdvlqkeidevyathptahealdngiveqhqqfvrsltevnggcavisdlsnrksyvtvhpwanflglt peeaalsvidsmdedciyrrihpedlvekrlmeykffqktfsmspgerlkyrgrcrlrmmnekgvyqyi dnlvqimqntpagnvwlifclyslsadqrpeqgiyatitqmergevetlslseehrnilserekeilrc irkglsskeiaatlyisvntvnrhrqnileklsvgnsieacraaelmkll | | | BLAST FFAS | | Structure Determination | | Method | XRAY | Chains | 3 | | Resolution (Å) | 2.04 | Rfree | 0.217 | | Matthews' coefficent | 3.64 | Rfactor | 0.187 | | Waters | 494 | Solvent Content | 66.25 |
| Ligand Information | | Ligands | | | Metals | | | |
Protein Summary
NP_811094.1 contains two domains (1-197, 198-257). The C-terminal domain contains a
LuxR DNA binding domain and has well defined structural homologs (rmsd<1 and seq id ~30), the N-terminal domain seems to be novel. There are no known structures which are highly homologous to the N-terminal domain.
This protein is likely to function as a dimer. The two DNA binding domains of NP_811094.1 are placed in an interesting fashion. By superimposing the
LuxR domains of this proteins and NarL-C/DNA complex, two strands of dsDNA can be approximately positioned onto NP_811094.1. Thus it appears that this protein severly bends the dsDNA or that it has to bind to separate strands of dsDNA.

Fig 1. NP_811094.1 with modeled dsDNA
This protein is likely to function as transcription regulator. The N-terminal domain can bind small molecule substrate. There are very few known sequence homologs for the N-terminal domain. It is thus not easy to infer whether it is the substrate binding site.

Fig 2. Sequence conservation on NP_811094.1 dimer surface. cyan-least conserved, magenta-most conserved residues.
Ligand Summary
References