MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it Conformational changes upon ligand binding in the essential class II fumarase Rv1098c from Mycobacterium tuberculosis. Conformational changes upon ligand binding in the essential class II fumarase Rv1098c from Mycobacterium tuberculosis. FEBS Lett. (0014-5793) 2012 Mechaly AE., Haouz A., Miras I., Barilone N., Weber P., Shepard W., Alzari PM., Bellinzoni M. suggested by lperfetto in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Mechaly AE., Haouz A., Miras I., Barilone N., Weber P., Shepard W., Alzari PM., Bellinzoni M. suggested by lperfetto FEBS Lett. (0014-5793) 2012 fumc_myctu Fumarate hydratase class II fumC fum MTV017.51c Rv1098c Aerobic fumarase Iron-independent fumarase protein protein myctu Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) MAVDADSANYRIEHDTMGEVRVPAKALWRAQTQRAVENFPISGRGLERTQIRALGLLKGACAQVNSDLGLLAPEKADAIIAAAAEIADGQHDDQFPIDVFQTGSGTSSNMNTNEVIASIAAKGGVTLHPNDDVNMSQSSNDTFPTATHIAATEAAVAHLIPALQQLHDALAAKALDWHTVVKSGRTHLMDAVPVTLGQEFSGYARQIEAGIERVRACLPRLGELAIGGTAVGTGLNAPDDFGVRVVAVLVAQTGLSELRTAANSFEAQAARDGLVEASGALRTIAVSLTKIANDIRWMGSGPLTGLAEIQLPDLQPGSSIMPGKVNPVLPEAVTQVAAQVIGNDAAIAWGGANGAFELNVYIPMMARNILESFKLLTNVSRLFAQRCIAGLTANVEHLRRLAESSPSIVTPLNSAIGYEEAAAVAKQALKERKTIRQTVIDRGLIGDRLSIEDLDRRLDVLAMAKAEQLDSDRL mint 4052F93F963D3DBB fumc-1 1 Rv1098c 2 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 4.0 direct interaction direct interaction mint t1 f1 f2 f3 Coordinates and structure factors have been deposited in the Protein Data Bank under the accession codes 4ADL (L-malate complex), 4ADM (meso-tartrate complex), 4APA (S318A mutant) and 4APB (S318C mutant in complex with fumarate). As expected for a class II fumarase, the enzyme assembles as an homo-tetramer.