4wd3

Crystal structure of an L-amino acid ligase RizA

spinqualitylabelsall models 4wd3, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4wd3 is a 2 chain structure with sequence from Bacillus subtilis subsp. subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.8Å Ligands: MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RIZA_BACIU Catalyzes the synthesis of Arg-Xaa dipeptides in an ATP-dependent manner. Has strict specificity toward arginine as the N-terminal substrate. Publication Abstract from PubMed RizA is an L-amino-acid ligase from Bacillus subtilis that participates in the biosynthesis of rhizocticin, an oligopeptide antibiotic. The substrate-free form of RizA has been crystallized and the structure was solved at 2.8 A resolution. The amino-acid-binding site appears to be capable of accommodating multiple amino acids, consistent with previous biochemical studies. Structure of RizA, an L-amino-acid ligase from Bacillus subtilis.,Kagawa W, Arai T, Ishikura S, Kino K, Kurumizaka H Acta Crystallogr F Struct Biol Commun. 2015 Sep;71(Pt 9):1125-30. doi:, 10.1107/S2053230X15012698. Epub 2015 Aug 25. PMID:26323296 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA