| Title | Crystal structure of acireductone dioxygenase (ARD) from Mus musculus at 2.06 angstrom resolution. Proteins 64 808-813 2006 | | Site | JCSG | | PDB Id | | Target Id | 354741 | | Molecular Characteristics | | Source | Mus musculus | | Alias Ids | TPS1340,13543033 | Molecular Weight | 21522.48 Da. | | Residues | 179 | Isoelectric Point | 5.31 | | Sequence | mvqawymdestadprkphraqpdrpvsleqlrtlgvlywkldadkyendpelekirkmrnyswmdiiti ckdtlpnyeekikmffeehlhldeeiryilegsgyfdvrdkedkwirismekgdmitlpagiyhrftld eknyvkamrlfvgepvwtpynrpadhfdarvqymsflegta | | | BLAST FFAS | | Structure Determination | | Method | XRAY | Chains | 1 | | Resolution (Å) | 2.06 | Rfree | 0.19532 | | Matthews' coefficent | 3.71 | Rfactor | 0.16229 | | Waters | 169 | Solvent Content | 66.57 |
| Ligand Information | | Ligands | | | Metals | | | |
Protein Summary
Mouse enzyme aci-reductone dioxygenase (ARD; GI: 13543033, EC 1.13.11.-,
Pfam03079), belongs to the superfamily of metal-containing RmlC-like cupins (PubMed:
16783794). ARD represents a branch point in the methionine salvage pathway leading from 5-methylthioadenosine (MTA) to methionine and catalyzes different reactions, depending on the type of metal ion bound in the active site (PubMed:11371200, 9880484).
Proteins from this family, such as immediate-early ethylene response gene OsARD1 (PubMed:16297065) were proposed to be part of early feedback activation of the methionine cycle by low
levels of ethylene to ensures the high and continuous rates of ethylene
synthesis required for long-term ethylene-mediated submergence
adaptation without depleting the tissue of AdoMet. OsARD was also found to be novel water-deficit-suppressed gene (PMID: 16169685). Another member of ARD family - membrane-type 1 matrix metalloproteinase cytoplasmic tail binding protein-1 (MTCBP-1) acts as an eukaryotic aci-reductone dioxygenase (ARD) in the methionine salvage pathway (PMID: 15938715) and is possible multifunctional protein acting as an invasion suppressor down-regulated in tumors (PubMed:
14718544). Protein Sip-L (from ARD protein family) was identified as cellular factors that was capable of supporting hepatitis C virus replication in 293EBNA cells (PMID: 11602742). The mRNA of another protein (GenBank:AAC08430, gi2996183) from ARD protein family is abundant in the third stage larvae of the parasitic nematode,
Ostertagia ostertagi (PubMed:
10769181).
ARD structure is typified by two antiparallel beta-sheets that form a cup-shaped, beta-sandwich jelly roll and has structure similar to RmlC-like cupins superfamily.
Ligand Summary
References