2BRA
Structure of N-Terminal FAD Binding motif of mouse MICAL
Summary for 2BRA
| Entry DOI | 10.2210/pdb2bra/pdb |
| Related | 2BRY 2C4C |
| Descriptor | NEDD9 INTERACTING PROTEIN WITH CALPONIN HOMOLOGY AND LIM DOMAINS, FLAVIN-ADENINE DINUCLEOTIDE, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | transport, axon guidance, vesicle transport, flavoprotein, redox, plexin, coiled coil, cytoskeleton, fad, lim domain, metal-binding, zinc |
| Biological source | MUS MUSCULUS (MOUSE) |
| Cellular location | Cytoplasm : Q8VDP3 |
| Total number of polymer chains | 2 |
| Total formula weight | 108515.15 |
| Authors | Nadella, M.,Bianchet, M.A.,Gabelli, S.B.,Amzel, L.M. (deposition date: 2005-05-04, release date: 2005-11-01, Last modification date: 2024-05-08) |
| Primary citation | Nadella, M.,Bianchet, M.A.,Gabelli, S.B.,Barrila, J.,Amzel, L.M. Structure and activity of the axon guidance protein MICAL. Proc. Natl. Acad. Sci. U.S.A., 102:16830-16835, 2005 Cited by PubMed Abstract: During development, neurons are guided to their targets by short- and long-range attractive and repulsive cues. MICAL, a large multidomain protein, is required for the combined action of semaphorins and plexins in axon guidance. Here, we present the structure of the N-terminal region of MICAL (MICAL(fd)) determined by x-ray diffraction to 2.0 A resolution. The structure shows that MICAL(fd) is an FAD-containing module structurally similar to aromatic hydroxylases and amine oxidases. In addition, we present biochemical data that show that MICAL(fd) is a flavoenzyme that in the presence of NADPH reduces molecular oxygen to H(2)O(2) (K(m,NAPDH) = 222 microM; k(cat) = 77 sec(-1)), a molecule with known signaling properties. We propose that the H(2)O(2) produced by this reaction may be one of the signaling molecules involved in axon guidance by MICAL. PubMed: 16275926DOI: 10.1073/pnas.0504838102 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
Download full validation report






