6KFS
Structure of CCM related protein
Summary for 6KFS
| Entry DOI | 10.2210/pdb6kfs/pdb |
| Descriptor | LCIB_C_CA domain-containing protein, ZINC ION (3 entities in total) |
| Functional Keywords | carbonic anhydrase, proton shuttle, metal binding protein |
| Biological source | Phaeodactylum tricornutum (Diatom) |
| Total number of polymer chains | 1 |
| Total formula weight | 28463.39 |
| Authors | |
| Primary citation | Jin, S.,Vullo, D.,Bua, S.,Nocentini, A.,Supuran, C.T.,Gao, Y.G. Structural and biochemical characterization of novel carbonic anhydrases from Phaeodactylum tricornutum. Acta Crystallogr D Struct Biol, 76:676-686, 2020 Cited by PubMed Abstract: Carbonic anhydrases (CAs) are a well characterized family of metalloenzymes that are highly efficient in facilitating the interconversion between carbon dioxide and bicarbonate. Recently, CA activity has been associated with the LCIB (limiting CO-inducible protein B) protein family, which has been an interesting target in aquatic photosynthetic microorganisms. To gain further insight into the catalytic mechanism of this new group of CAs, the X-ray structure of a highly active LCIB homolog (PtLCIB3) from the diatom Phaeodactylum tricornutum was determined. The CA activities of PtLCIB3, its paralog PtLCIB4 and a variety of their mutants were also measured. It was discovered that PtLCIB3 has a classic β-CA fold and its overall structure is highly similar to that of its homolog PtLCIB4. Subtle structural alterations between PtLCIB3 and PtLCIB4 indicate that an alternative proton-shuttle cavity could perhaps be one reason for their remarkable difference in CA activity. A potential alternative proton-shuttle route in the LCIB protein family is suggested based on these results. PubMed: 32627740DOI: 10.1107/S2059798320007202 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.2 Å) |
Structure validation
Download full validation report
