1Z6K
Citrate lyase beta subunit complexed with oxaloacetate and magnesium from M. tuberculosis
Summary for 1Z6K
Entry DOI | 10.2210/pdb1z6k/pdb |
Related | 1SGJ 1U5H |
Descriptor | Citrate Lyase beta subunit, OXALOACETATE ION, MAGNESIUM ION, ... (4 entities in total) |
Functional Keywords | tim barrel, structural genomics, psi, protein structure initiative, tb structural genomics consortium, tbsgc, lyase |
Biological source | Mycobacterium tuberculosis |
Total number of polymer chains | 1 |
Total formula weight | 31575.78 |
Authors | Goulding, C.W.,Bowers, P.M.,Segelke, B.,Lekin, T.,Kim, C.Y.,Terwilliger, T.C.,Eisenberg, D.,TB Structural Genomics Consortium (TBSGC) (deposition date: 2005-03-22, release date: 2005-05-03, Last modification date: 2024-10-30) |
Primary citation | Goulding, C.W.,Bowers, P.M.,Segelke, B.,Lekin, T.,Kim, C.Y.,Terwilliger, T.C.,Eisenberg, D. The structure and computational analysis of Mycobacterium tuberculosis protein CitE suggest a novel enzymatic function. J.Mol.Biol., 365:275-283, 2007 Cited by PubMed Abstract: Fatty acid biosynthesis is essential for the survival of Mycobacterium tuberculosis and acetyl-coenzyme A (acetyl-CoA) is an essential precursor in this pathway. We have determined the 3-D crystal structure of M. tuberculosis citrate lyase beta-subunit (CitE), which as annotated should cleave protein bound citryl-CoA to oxaloacetate and a protein-bound CoA derivative. The CitE structure has the (beta/alpha)(8) TIM barrel fold with an additional alpha-helix, and is trimeric. We have determined the ternary complex bound with oxaloacetate and magnesium, revealing some of the conserved residues involved in catalysis. While the bacterial citrate lyase is a complex with three subunits, the M. tuberculosis genome does not contain the alpha and gamma subunits of this complex, implying that M. tuberculosis CitE acts differently from other bacterial CitE proteins. The analysis of gene clusters containing the CitE protein from 168 fully sequenced organisms has led us to identify a grouping of functionally related genes preserved in M. tuberculosis, Rattus norvegicus, Homo sapiens, and Mus musculus. We propose a novel enzymatic function for M. tuberculosis CitE in fatty acid biosynthesis that is analogous to bacterial citrate lyase but producing acetyl-CoA rather than a protein-bound CoA derivative. PubMed: 17064730DOI: 10.1016/j.jmb.2006.09.086 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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