7dbs

Crystal Structure Of Biotin Protein Ligase From Leishmania Major in complex with Biotin

spinqualitylabelsall models 7dbs, resolution 2.33Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7dbs is a 1 chain structure with sequence from Leishmania major. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.33Å Ligands: BTN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q4Q6F6_LEIMA Publication Abstract from PubMed Biotin protein ligase catalyses the post-translational modification of biotin carboxyl carrier protein (BCCP) domains, a modification that is crucial for the function of several carboxylases. It is a two-step process that results in the covalent attachment of biotin to the -amino group of a conserved lysine of the BCCP domain of a carboxylase in an ATP-dependent manner. In Leishmania, three mitochondrial enzymes, acetyl-CoA carboxylase, methylcrotonyl-CoA carboxylase and propionyl-CoA carboxylase, depend on biotinylation for activity. In view of the indispensable role of the biotinylating enzyme in the activation of these carboxylases, crystal structures of L. major biotin protein ligase complexed with biotin and with biotinyl-5'-AMP have been solved. L. major biotin protein ligase crystallizes as a unique dimer formed by cross-handshake interactions of the hinge region of the two monomers formed by partial unfolding of the C-terminal domain. Interestingly, the substrate (BCCP domain)-binding site of each monomer is occupied by its own C-terminal domain in the dimer structure. This was observed in all of the crystals that were obtained, suggesting a closed/inactive conformation of the enzyme. Size-exclusion chromatography studies carried out using high protein concentrations (0.5 mM) suggest the formation of a concentration-dependent dimer that exists in equilibrium with the monomer. Leishmania major biotin protein ligase forms a unique cross-handshake dimer.,Rajak MK, Bhatnagar S, Pandey S, Kumar S, Verma S, Patel AK, Sundd M Acta Crystallogr D Struct Biol. 2021 Apr 1;77(Pt 4):510-521. doi:, 10.1107/S2059798321001418. Epub 2021 Mar 30. PMID:33825711 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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