{"entry": {"accession": "MF7000212", "general": {"name": "Chorismate mutase (Mycobacterium tuberculosis)", "pdb_id": "2qbv", "exp_method": "X-ray", "resolution": "2.00", "assembly": "Homodimer", "source_organism": "Mycobacterium tuberculosis", "publication": {"pmid": "18727669", "authors": "Kim SK, Reddy SK, Nelson BC, Robinson H, Reddy PT, Ladner JE", "title": "A comparative biochemical and structural analysis of the intracellular chorismate mutase (Rv0948c) from Mycobacterium tuberculosis H(37)R(v) and the secreted chorismate mutase (y2828) from Yersinia pestis.", "journal": "FEBS J.", "year": "2008", "issue": "19", "volume": "275", "pages": "4824-35", "abstract": "The Rv0948c gene from Mycobacterium tuberculosis H(37)R(v) encodes a 90 amino acid protein as the natural gene product with chorismate mutase (CM) activity. The protein, 90-MtCM, exhibits Michaelis-Menten kinetics with a k(cat) of 5.5+/-0.2s(-1) and a K(m) of 1500+/-100microm at 37 degrees C and pH7.5. The 2.0A X-ray structure shows that 90-MtCM is an all alpha-helical homodimer (Protein Data Bank ID: 2QBV) with the topology of Escherichia coli CM (EcCM), and that both protomers contribute to each catalytic site. Superimposition onto the structure of EcCM and the sequence alignment shows that the C-terminus helix3 is shortened. The absence of two residues in the active site of 90-MtCM corresponding to Ser84 and Gln88 of EcCM appears to be one reason for the low k(cat). Hence, 90-MtCM belongs to a subfamily of alpha-helical AroQ CMs termed AroQ(delta.) The CM gene (y2828) from Yersinia pestis encodes a 186 amino acid protein with an N-terminal signal peptide that directs the protein to the periplasm. The mature protein, *YpCM, exhibits Michaelis-Menten kinetics with a k(cat) of 70+/-5s(-1) and K(m) of 500+/-50microm at 37 degrees C and pH7.5. The 2.1A X-ray structure shows that *YpCM is an all alpha-helical protein, and functions as a homodimer, and that each protomer has an independent catalytic unit (Protein Data Bank ID: 2GBB). *YpCM belongs to the AroQ(gamma) class of CMs, and is similar to the secreted CM (Rv1885c, *MtCM) from M.tuberculosis."}}, "function": {"molecular_function": {"go": {"accession": "GO:0004106", "name": "chorismate mutase activity"}}, "cellular_component": {"go": [{"accession": "GO:0005737", "name": "cytoplasm"}, {"accession": "GO:0005886", "name": "plasma membrane"}]}, "biological_process": {"go": [{"accession": "GO:0008652", "name": "amino acid biosynthetic process"}, {"accession": "GO:0009095", "name": "aromatic amino acid family biosynthetic process, prephenate pathway"}, {"accession": "GO:0046417", "name": "chorismate metabolic process"}, {"accession": "GO:0009697", "name": "salicylic acid biosynthetic process"}]}}, "macromolecules": {"general": {"nr_of_chains": "2", "nr_of_unique_protein_segments": "1", "class": "Homooligomeric enzymes", "subclass": "Homodimeric enzymes", "note": "All chains according to the most probable oligomerization state stored in PDBe were considered."}, "chain": [{"id": "A", "name": "Intracellular chorismate mutase", "source_organism": "Mycobacterium tuberculosis", "uniprot": {"id": "P9WIC1", "start": "28", "end": "100", "coverage": "69%", "sequence": "MRPEPPHHENAELAAMNLEMLESQPVPEIDTLREEIDRLDAEILALVKRRAEVSKAIGKARMASGGTRLVHSREMKVIERYSELGPDGKDLAILLLRLGRGRLGH", "length": "105"}, "regions": {"region": [{"region_type": "secondary structure", "region_name": "helix", "region_start": "13", "region_end": "48"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "57", "region_end": "67"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "70", "region_end": "84"}, {"region_type": "pfam", "region_id": "PF01817", "region_name": "Chorismate mutase type II", "region_start": "32", "region_end": "88"}]}}, {"id": "A-2", "name": "Intracellular chorismate mutase", "source_organism": "Mycobacterium tuberculosis", "uniprot": {"id": "P9WIC1", "start": "28", "end": "100", "coverage": "69%", "sequence": "MRPEPPHHENAELAAMNLEMLESQPVPEIDTLREEIDRLDAEILALVKRRAEVSKAIGKARMASGGTRLVHSREMKVIERYSELGPDGKDLAILLLRLGRGRLGH", "length": "105"}, "regions": {"region": {"region_type": "pfam", "region_id": "PF01817", "region_name": "Chorismate mutase type II", "region_start": "32", "region_end": "88"}}}]}, "evidence": {"evidence_level": "Indirect evidence", "evidence_coverage": "The full structure participates in mutual synergistic folding.", "sequence_domain": "Chorismate mutase type II", "complex_evidence": "The enzyme is an intertwined dimer of three helices with connecting loops. The N-terminal helices of the two monomers twine together to form an anti-parallel coiled-coil with a hydrophobic interaction surface. The loop between the first and second helices is disordered (PMID:16914555).", "chain_evidence": [{"chain_id": "A", "support": "N/A"}, {"chain_id": "A-2", "support": "N/A"}]}, "related_structures": {"id": ["MF7000162", "MF7000212", "MF7000163", "MF7000211", "MF7000164", "MF7000165", "MF7000209", "MF7000210"]}}}