1xg3
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1xg3 |SIZE=350|CAPTION= <scene name='initialview01'>1xg3</scene>, resolution 1.9Å | |PDB= 1xg3 |SIZE=350|CAPTION= <scene name='initialview01'>1xg3</scene>, resolution 1.9Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene> | + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Methylisocitrate_lyase Methylisocitrate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.30 4.1.3.30] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Methylisocitrate_lyase Methylisocitrate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.30 4.1.3.30] </span> |
|GENE= prpB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= prpB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1oqf|1oqf]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xg3 OCA], [http://www.ebi.ac.uk/pdbsum/1xg3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xg3 RCSB]</span> | ||
}} | }} | ||
| Line 29: | Line 32: | ||
[[Category: Lu, Z.]] | [[Category: Lu, Z.]] | ||
[[Category: Melamud, E.]] | [[Category: Melamud, E.]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: PYR]] | ||
| - | [[Category: SIN]] | ||
[[Category: 2-methylisocitrate lyase/product complex]] | [[Category: 2-methylisocitrate lyase/product complex]] | ||
[[Category: isocitrate lyase superfamily]] | [[Category: isocitrate lyase superfamily]] | ||
| Line 37: | Line 37: | ||
[[Category: succinate]] | [[Category: succinate]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:49:08 2008'' |
Revision as of 21:49, 30 March 2008
| |||||||
| , resolution 1.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | prpB (Escherichia coli) | ||||||
| Activity: | Methylisocitrate lyase, with EC number 4.1.3.30 | ||||||
| Related: | 1oqf
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the C123S 2-methylisocitrate lyase mutant from Escherichia coli in complex with the reaction product, Mg(II)-pyruvate and succinate
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
1XG3 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 Mon Mar 31 00:49:08 2008
