1oqf

<table><tr><td colspan='2'>[[1oqf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OQF OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1OQF FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PRPB OR B0331 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1oqf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oqf OCA], [http://pdbe.org/1oqf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1oqf RCSB], [http://www.ebi.ac.uk/pdbsum/1oqf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1oqf ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/PRPB_ECOLI PRPB_ECOLI]] Catalyzes the formation of pyruvate and succinate from 2-methylisocitrate.<ref>PMID:11422389</ref> <ref>PMID:15723538</ref>

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:15723538</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1oqf" style="background-color:#fffaf0;"></div>

[[Category: Bacillus coli migula 1895]]

[[Category: Dunaway-Mariano, D]]

[[Category: Herzberg, O]]

[[Category: Liu, S]]

[[Category: Lu, Z]]

[[Category: Swapped helix across a dimer]]