| Title | Crystal structure of a cysteine protease (BDI_2249) from Parabacteroides distasonis ATCC 8503 at 2.23 A resolution. To be published | | Site | JCSG | | PDB Id | | Target Id | 394726 | | Molecular Characteristics | | Source | Parabacteroides distasonis atcc 8503 | | Alias Ids | TPS25828,YP_001303602.1 | Molecular Weight | 43457.71 Da. | | Residues | 382 | Isoelectric Point | 5.49 | | Sequence | dtekkvseegfvfttvkenpitsvknqnragtcwcyssysflesellrmgkgeydlsemftvyntyldr adaavrthgdvsfsqggsfydalygmetfglvpeeemrpgmmyadtlsnhtelsaltdamvaaiakgkl rklqsdennamlwkkavaavhqiylgvppekftykgkeytpksffestglkasdyvsltsythhpfytq fpleiqdnwrhgmsynlpldefmevfdnaintgytiawgsdvsesgftrdgvavmpddekvqelsgsdm ahwlklkpeekklntkpqpqkwctqaerqlaydnyettddhgmqiygiakdqegneyymvknswgtnsk yngiwyaskafvryktmnivvhkdalpkaikaklgik | | | BLAST FFAS | | Structure Determination | | Method | XRAY | Chains | 3 | | Resolution (Å) | 2.23 | Rfree | 0.1812 | | Matthews' coefficent | 3.03 | Rfactor | 0.1592 | | Waters | 2007 | Solvent Content | 59.37 |
| Ligand Information | | Ligands | | | Metals | | | |
Protein Summary
First structure of bacterial Peptidase C1B (PF03051), a member of bleomycin hydrolase family and a Peptidase_CA (CL0125) clan. Multiple eukaryotic (yeast and human) structures were solved previously. Despite low sequence level similarity (~18% seq id) the structure is very similar to yeast bleomycin hydrolase and other cysteine proteinases. This family of peptidase functions as a hexamer.
BDI_2249 is predicted to be secreted, possibly anchored in the outer membrane. Its exact function is unknown, possibly involved in extracellular protein degradation. Proteins from this family are abundant in all gut microbiome bacteroides, but also (more distant) in a wide variety of bacteria, with usually at least three paralogs in each genome. A distant homolog from S. thermophilus was purified and experimentally characterized [Ref].
Ligand Summary