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 http://mint.bio.uniroma2.it/mint anonymous-2014za-1 Crystal structure of an efficacious gonococcal adherence inhibitor: an enolase from Lactobacillus gasseri in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined raghuna1@msu.edu 2014 imex curation Raghunathan K., Harris P.T., Spurbeck R.R., Arvidson C.G., Arvidson D.N. FEBS Lett. (0014-5793) Only protein-protein interactions d1yhf0_lacgs Enolase eno 2-phospho-D-glycerate hydro-lyase 2-phosphoglycerate dehydratase HMPREF9209_0508 protein protein lactobacillus gasseri 224-1 lactobacillus gasseri 224-1 MSVITDIHAREVLDSRGNPTVEAEVYTELGGFGRAIVPSGASTGEHEAVELRDGDKSRFGGQGVLTAVENVNGEIAKAVIGLDVTDQRLIDQTMIDLDGTPNKGRLGANAILSVSLASARAAADELGLPLYEYLGGPNAHVLPTPMMNVINGGKHADNNVDIQEFMIMPVGAKSLHEAVRMGAETFHTLKGLLQERGESTAVGDEGGFAPNLKNNEEPFEILVEAIQRAGYKPGQDIAIAFDCAASEFYNKDTKKYVTVADGREYTAEEWTSLIEDLVDKYPVISVEDPLDENDWEGWKTFTERLGDKVQIVGDDLFVTNTSYLEKGIKMGVANSILIKLNQIGTLTETFEAIEMAKEAGYTAVVSHRSGETEDTTIADLVVATNAGQIKTGSMSRTDRIAKYNQLMRIEEALGSTAQYKGIHSFYNLHKQF eno-1 1538044 n/a 1538045 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.0 direct interaction direct interaction false false false t1 f1 f2a Analysis of the structure estimated 15000 Å2 of solvent accessible surface area per monomer, with a 1530 Å2 monomer-monomer interface. The octameric assembly implied by symmetry consists of a tetramer of dimers much like the enolase structures derived from S. pneumoniae (1W6T) and S. suis (4EWJ). This assembly has an 1190 Å2 dimer-dimer interface. Inspecting the residues that are at least 70% buried (a symmetric set of 13 residues per monomer) showed significant conservation with the known octameric enolases 1W6T and 4EWJ, suggesting the octamer is biologically significant and not an artifact from crystal packing.