1oqf
From Proteopedia
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'''Crystal structure of the 2-methylisocitrate lyase''' | '''Crystal structure of the 2-methylisocitrate lyase''' | ||
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[[Category: Lu, Z.]] | [[Category: Lu, Z.]] | ||
[[Category: S2F, Structure 2.Function Project.]] | [[Category: S2F, Structure 2.Function Project.]] | ||
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| - | [[Category: | + | [[Category: Structural genomic]] |
| - | [[Category: | + | [[Category: Structure 2 function project]] |
| - | [[Category: | + | [[Category: Swapped helix across a dimer]] |
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Revision as of 01:09, 3 May 2008
Crystal structure of the 2-methylisocitrate lyase
Overview
Two crystal structures of the C123S mutant of 2-methylisocitrate lyase have been determined, one with the bound reaction products, Mg(2+)-pyruvate and succinate, and the second with a bound Mg(2+)-(2R,3S)-isocitrate inhibitor. Comparison with the structure of the wild-type enzyme in the unbound state reveals that the enzyme undergoes a conformational transition that sequesters the ligand from solvent, as previously observed for two other enzyme superfamily members, isocitrate lyase and phosphoenolpyruvate mutase. The binding modes reveal the determinants of substrate specificity and stereoselectivity, and the stringent specificity is verified in solution using various potential substrates. A model of bound 2-methylisocitrate has been developed based on the experimentally determined structures. We propose a catalytic mechanism involving an alpha-carboxy-carbanion intermediate/transition state, which is consistent with previous stereochemical experiments showing inversion of configuration at the C(3) of 2-methylisocitrate. Structure-based sequence analysis and phylogenic tree construction reveal determinants of substrate specificity, highlight nodes of divergence of families, and predict enzyme families with new functions.
About this Structure
1OQF is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structures of 2-methylisocitrate lyase in complex with product and with isocitrate inhibitor provide insight into lyase substrate specificity, catalysis and evolution., Liu S, Lu Z, Han Y, Melamud E, Dunaway-Mariano D, Herzberg O, Biochemistry. 2005 Mar 1;44(8):2949-62. PMID:15723538 Page seeded by OCA on Sat May 3 04:09:32 2008
