1m6j

<table><tr><td colspan='2'>[[1m6j]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Enthi Enthi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M6J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M6J FirstGlance]. <br>

</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m6j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m6j OCA], [http://pdbe.org/1m6j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1m6j RCSB], [http://www.ebi.ac.uk/pdbsum/1m6j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1m6j ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Triosephosphate isomerase (TIM) has been proposed as a target for drug design. TIMs from several parasites have a cysteine residue at the dimer interface, whose derivatization with thiol-specific reagents induces enzyme inactivation and aggregation. TIMs lacking this residue, such as human TIM, are less affected. TIM from Entamoeba histolytica (EhTIM) has the interface cysteine residue and presents more than ten insertions when compared with the enzyme from other pathogens. To gain further insight into the role that interface residues play in the stability and reactivity of these enzymes, we determined the high-resolution structure and characterized the effect of methylmethane thiosulfonate (MMTS) on the activity and conformational properties of EhTIM. The structure of this enzyme was determined at 1.5A resolution using molecular replacement, observing that the dimer is not symmetric. EhTIM is completely inactivated by MMTS, and dissociated into stable monomers that possess considerable secondary structure. Structural and spectroscopic analysis of EhTIM and comparison with TIMs from other pathogens reveal that conformational rearrangements of the interface after dissociation, as well as intramonomeric contacts formed by the inserted residues, may contribute to the unusual stability of the derivatized EhTIM monomer.

Structure and inactivation of triosephosphate isomerase from Entamoeba histolytica.,Rodriguez-Romero A, Hernandez-Santoyo A, del Pozo Yauner L, Kornhauser A, Fernandez-Velasco DA J Mol Biol. 2002 Sep 27;322(4):669-75. PMID:12270704<ref>PMID:12270704</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 1m6j" style="background-color:#fffaf0;"></div>

*[[Triose Phosphate Isomerase|Triose Phosphate Isomerase]]

[[Category: Enthi]]

[[Category: Fernandez-Velasco, D A]]

[[Category: Hernandez-Santoyo, A]]

[[Category: Rodriguez-Romero, A]]

[[Category: Triosephosphate isomerase]]