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 Structural and functional characterization of a novel type-III dockerin from Ruminococcus flavefaciens. Structural and functional characterization of a novel type-III dockerin from Ruminococcus flavefaciens. FEBS Lett. (0014-5793) 2013 Karpol A., Jobby MK., Slutzki M., Noach I., Chitayat S., Smith SP., Bayer EA. in vitro In vitro elisa enzyme linked immunosorbent assay ELISA ELISA elisa predetermined predetermined participant predetermined Karpol A., Jobby MK., Slutzki M., Noach I., Chitayat S., Smith SP., Bayer EA. FEBS Lett. (0014-5793) 2013 Structural and functional characterization of a novel type-III dockerin from Ruminococcus flavefaciens. Structural and functional characterization of a novel type-III dockerin from Ruminococcus flavefaciens. FEBS Lett. (0014-5793) 2013 Karpol A., Jobby MK., Slutzki M., Noach I., Chitayat S., Smith SP., Bayer EA. in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Karpol A., Jobby MK., Slutzki M., Noach I., Chitayat S., Smith SP., Bayer EA. FEBS Lett. (0014-5793) 2013 Structural and functional characterization of a novel type-III dockerin from Ruminococcus flavefaciens. Structural and functional characterization of a novel type-III dockerin from Ruminococcus flavefaciens. FEBS Lett. (0014-5793) 2013 Karpol A., Jobby MK., Slutzki M., Noach I., Chitayat S., Smith SP., Bayer EA. in vitro In vitro biophysical biophysical predetermined predetermined participant predetermined Karpol A., Jobby MK., Slutzki M., Noach I., Chitayat S., Smith SP., Bayer EA. FEBS Lett. (0014-5793) 2013 Structural and functional characterization of a novel type-III dockerin from Ruminococcus flavefaciens. Structural and functional characterization of a novel type-III dockerin from Ruminococcus flavefaciens. FEBS Lett. (0014-5793) 2013 Karpol A., Jobby MK., Slutzki M., Noach I., Chitayat S., Smith SP., Bayer EA. in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Karpol A., Jobby MK., Slutzki M., Noach I., Chitayat S., Smith SP., Bayer EA. FEBS Lett. (0014-5793) 2013 q9ae53_rumfl scaA protein protein ruminococcus flavefa Ruminococcus flavefaciens MKKLISAVTSLCMAATMVSVVAPSTVGAADTAKGFAVKTYDADKPSSADGKSTVTIDKKDIPASGYTFPAALYYSEESASTTSFLVHLTTDSSAITFPKVYEPDQPYFSAEKEQVMASGTASTDCYVSFGGQLSKRGKYSAAGLAKFGLDSSQSAAGTDNYFLGCSWMNMGEEYTWAGAKSDSFPVYVFDVNIPATIAAGTYHITYCKYDTDPDPANEVMAPMAEAKTNDVKSKYNLASNNLKLEEMTIVVTENGSTPGTTTTVTQPPVTTTTTVGTVTPGDKDFNFKFVDDKGNSVVSANPGDEITVCVQVDAGNNTCAGMDVKFNTSGLAIDEFENNSEACGNAKLAKNEKEFRANFTSTGTDGEPMKVSNGKDAFTFYVTIPATAKDTSYTIGFVDGELNVFKEGGTGSKYTAGYTPLTINVGTPNPGTTTTVTQPPVTTTTTGGQTSNADFKFSFVDDKGQSTVNAKAGDEITVCVQVDAGNNTCAGMDVQFSTSGLAIDEFENNSEACGNAKLAKNEKELRANFTSTGTDGEPMKVSNGKDAFTFYVTIPAYAKDTYYVIGFVDSELNVFKEGGTGDNTIAFYTPLTINGTPNPGTTSTVTQPPVTTTTTGGQTSNAEFKFSFVDDKDQSAINVNAGDEVTVCVKVDAGNNTCAGMDVQFSTSGLAIDEFENNSEACGNAKLAKNEKELRANFTSTGTDGEPMKVSNGKDAFTFYVTIPATAKDGDTYKIGFVDSELKVFKEGGTGDKYTASYTPLTITVGKQPVTTSTTTTTVTTTSTTTTTVTTPQPGTKLVPTWGDTNCDGVVNVADVVVLNRFLNDPTYSNITDQGKVNADVVDPQDKSGAAVDPAGVKLTVADSEAILKAIVELITLPQ mint 76577506C4820D7D q9ae52_rumfl scaB protein protein ruminococcus flavefa Ruminococcus flavefaciens MKKLLSAVTSVAMSFTLMAGAFASSVSAAGGLSAVQPNVSLGEVLDVSANRTAADGTVEWLIPTVTAAPGQTVTMPVVVKSSSLAVAGAQFKIQAATGVRYSSKTDGDAYGSGIVYNNSKYAFGQGAGRGIVAADDSVVLTLAYTVPADCAEGTYDVKWSDAFVSDTDGQNITSKVTLTDGAIIVKKDNNTGKIKWVLDKVTAAPGETVTVKATVDASGEGTVAVAGAQFDVNADSPIVYDSAKEGGAYITSLTVNDAKHKFAFGRTTGTGIVAADKATVAAFTYKVPSDCTEGTYDVKWSGGFVSDADGKDITSRVTFVDGSITVKNDVQTVGKWVLDNVTAAQGETVTLKAVVDDSAKAAVPVAGAQFKLQAADAVKYSSFTDGTAYGAAFTKNDDKQSFAFGNTGGKGVAAADKAAIYTVSYTVPTDCPDGTYPVKWADTFVSDTDGRNITSNIIFVDGSITVGKPVTGTVEWVIPKVDADAGDNVTLQVAVKGDADLPVSAAQFDVNGATPLNYQESAGKPYGVDLVVNDTKQHFAFAQASGISKTAKDGDKLFTITFKVPEDCADGIYPVTWAKQFVSDENGNNITDKVTFTDGWVRVGNPPTTTTTTTTSVTTTTTTTTVTAPKGGIIWAIDTVTVEPGQTATLNIKVVDEDNSKLPIAGAQFNIVNKDGVNYSSIAGSEAYGPTITANDAKKKFDFANASGVETVGANNANVAVLTYTVPATAEEGVYPVQFAEGSLKIFDKDGKDISDKIIGVDGAIIVKKPVVTDVTSTTTVTSNVNTTTSTTTVTAPQGGIIWAIDTVTVEPGQTATLNIKVVDLDNSQLPIAGAQFNIVNKDGVNYSSIAGSEAYGPKITANDAKKKFDFANASGVETVGANDAIVAVLTYTVPATAEEGVYPVQFAEGSLKIFDKDGKDISDKIIGVDGAIIVKKPVITETSTTTTVTGKPNTSTTTTTGTDVTTSGNETTDTTVTTVTTTDVTGPTTTSTDTTVTSSVVGPTTTSTIVTDTTVTSSVIGPTTTTTVVTDTTVTSSVIGPTTTTTVVTDTTVTSSVIGPTTTTTVVTDTTVTSSVIGPTTTTTVVTDTTVTSSVIGPTTTSTTVTTEVTGPTDTTATSTGTSTTDVTGPTDTTVTSTGTSTTDVTGPTDTTVTSTGTSTTDVTGPTDTTVTSTSTTTDVTGPTDTTVTDTTVTTVVTNPTTTLTTTTIVVPKDSIAWVVDTVAAYPGDEVTLKITVKDPNAANLGIAGAQFKVTPDGDVQLVKSGDKSGYGADIIPSKDGYKFVFADGAGVAHVAPDGTVVIELTYKVGEEVAPGTVIPVSIKDLYVVDEDGNDITKYVMPVDGSIIVFEKPAPTSTTTNVTVTTVTTDVTGPTDTTVTSTGTSTTDVTGPTDTTVTSTGTSTTDVTGPTDTTVTSTSTTTDVTGPTDTTVTSTSTTTDVTGPTDTTVTSTSTTTDVTGPTDTTETSTSTTTDVTGPTTTSTTSTSTETTSTDTTTSTSTSSTSTTSTTDANYDHSYAVIETQVGYYFSHDDGVRANGQVGGFNKGQVVTLKIVDVYKDGSEVERPEVNMDLINFNNNTPEKAYNSRTHINKQTTITDFKYDIPVYYGDMPLVDKSGKALTVTAYIGVKGDITLSNMVDSNDASVALSYYTLISTGSNTPANTICQITEEGLQVSSALDELDNLAAFLGDVNTNEWDPDNWKTTKMGRKIDSNDASQILAFYSKRTSHVYDDVSSNDIWNEILGDARFGK AC4FCBD790DB5022 scaa-scab 4 ScaADoc 5 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Stoichiometry: 1.1 ScaB cohesin 6 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Stoichiometry: 1.1 direct interaction direct interaction f5b mint scaa-scab-1 2 ScaADoc 5 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Stoichiometry: 1.1 ScaB cohesin 6 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Stoichiometry: 1.1 direct interaction direct interaction f5a mint scaa-scab-2 3 ScaADoc 5 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ScaB cohesin 6 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction f6a mint Using differential scanning calorimetry (DSC) and ELISA-based analyses, we investigated whether the lack of Ca2+ coordination to the second F-hand variant disrupted the thermal and structural stabilities of the ScaADoc-cohesin complex. Analysis of the DSC data revealed that complex formation with ScaB cohesin stabilized Ca2+-bound ScaADoc as evidenced by a considerable shift in the melting temperature (Tm) from 61.80 °C to 90.05 °C (Figure 6A). This is in contrast to the thermostability of the ScaB cohesin, which appears to have the same Tm in its un- and complexed form. scab-scaa 1 ScaADoc 5 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role prey prey purified purified fusion protein fusion protein fusion protein undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined binding site binding region binding-associated region binding region deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ScaB cohesin 6 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role bait bait purified purified fusion protein fusion protein fusion protein undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction f6b mint Despite the thermostability of the ScaADoc-ScaB cohesin complex, the extreme sensitivity of C-terminal truncations on ScaADoc was realized when deletion of Ala1699-Thr1705 significantly abrogated binding to ScaB cohesin (Figure 6B).