2C7Z
Plant enzyme crystal form II
Summary for 2C7Z
| Entry DOI | 10.2210/pdb2c7z/pdb |
| Related | 2C7Y |
| Descriptor | 3-KETOACYL-COA THIOLASE 2 (2 entities in total) |
| Functional Keywords | fatty acid metabolism, transferase, oxylipin synthesis, lipid synthesis, acyltransferase |
| Biological source | ARABIDOPSIS THALIANA (MOUSE-EAR CRESS) |
| Cellular location | Peroxisome: Q9S7M3 |
| Total number of polymer chains | 1 |
| Total formula weight | 42265.40 |
| Authors | Sundaramoorthy, R.,Micossi, E.,Alphey, M.S.,Leonard, G.A.,Hunter, W.N. (deposition date: 2005-11-30, release date: 2006-05-17, Last modification date: 2024-11-06) |
| Primary citation | Sundaramoorthy, R.,Micossi, E.,Alphey, M.S.,Germain, V.,Bryce, J.H.,Smith, S.M.,Leonard, G.A.,Hunter, W.N. The Crystal Structure of a Plant 3-Ketoacyl-Coa Thiolase Reveals the Potential for Redox Control of Peroxisomal Fatty Acid Beta-Oxidation. J.Mol.Biol., 359:347-, 2006 Cited by PubMed Abstract: Crystal structures of peroxisomal Arabidopsis thaliana 3-ketoacyl-CoA thiolase (AtKAT), an enzyme of fatty acid beta-oxidation, are reported. The subunit, a typical thiolase, is a combination of two similar alpha/beta domains capped with a loop domain. The comparison of AtKAT with the Saccharomyces cerevisiae homologue (ScKAT) structure reveals a different placement of subunits within the functional dimers and that a polypeptide segment forming an extended loop around the open catalytic pocket of ScKAT converts to alpha-helix in AtKAT, and occludes the active site. A disulfide is formed between Cys192, on this helix, and Cys138, a catalytic residue. Access to Cys138 is determined by the structure of this polypeptide segment. AtKAT represents an oxidized, previously unknown inactive form, whilst ScKAT is the reduced and active enzyme. A high level of sequence conservation is observed, including Cys192, in eukaryotic peroxisomal, but not mitochondrial or prokaryotic KAT sequences, for this labile loop/helix segment. This indicates that KAT activity in peroxisomes is influenced by a disulfide/dithiol change linking fatty acid beta-oxidation with redox regulation. PubMed: 16630629DOI: 10.1016/J.JMB.2006.03.032 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.37 Å) |
Structure validation
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