NMR Studies on the Substrate-binding Domains of the Thermosome: Structural Plasticity in the Protrusion Region Export

@article{citeulike:2741358, abstract = {Group II chaperonins close their cavity with the help of conserved, helical extensions, the so-called protrusions, which emanate from the apical or substrate-binding domains. A comparison of previously solved crystal structures of the apical domains of the thermosome from Thermoplasma acidophilum showed structural plasticity in the protrusion parts induced by extensive packing interactions. In order to assess the influence of the crystal contacts we investigated both the [alpha] and [beta]-apical domains ([alpha]-ADT and [beta]-ADT) in solution by NMR spectroscopy. Secondary structure assignments and 15N backbone relaxation measurements showed mostly rigid structural elements in the globular parts of the domains, but revealed intrinsic structural disorder and partial helix fraying in the protrusion regions. On the other hand, a [beta]-turn-motif conserved in archaeal group II chaperonins might facilitate substrate recognition. Our results help us to specify the idea of the open, substrate-accepting state of the thermosome and may provide an additional jigsaw piece in understanding the mode of substrate binding of group II chaperonins.}, author = {Heller, Markus and John, Michael and Coles, Murray and Bosch, Gundula and Baumeister, Wolfgang and Kessler, Horst}, citeulike-article-id = {2741358}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.jmb.2003.12.035}, citeulike-linkout-1 = {http://www.sciencedirect.com/science/article/B6WK7-4BCWWHT-1/1/bd7c48bef531d43d2c3d439d8de33038}, day = {20}, doi = {10.1016/j.jmb.2003.12.035}, journal = {Journal of Molecular Biology}, keywords = {chemical-shift, cs-perturbation}, month = {February}, number = {3}, pages = {717--729}, posted-at = {2008-05-01 01:34:59}, priority = {1}, title = {NMR Studies on the Substrate-binding Domains of the Thermosome: Structural Plasticity in the Protrusion Region}, url = {http://dx.doi.org/10.1016/j.jmb.2003.12.035}, volume = {336}, year = {2004} }

TY - JOUR ID - citeulike:2741358 L3 - citeulike-article-id:2741358 N2 - Group II chaperonins close their cavity with the help of conserved, helical extensions, the so-called protrusions, which emanate from the apical or substrate-binding domains. A comparison of previously solved crystal structures of the apical domains of the thermosome from Thermoplasma acidophilum showed structural plasticity in the protrusion parts induced by extensive packing interactions. In order to assess the influence of the crystal contacts we investigated both the [alpha] and [beta]-apical domains ([alpha]-ADT and [beta]-ADT) in solution by NMR spectroscopy. Secondary structure assignments and 15N backbone relaxation measurements showed mostly rigid structural elements in the globular parts of the domains, but revealed intrinsic structural disorder and partial helix fraying in the protrusion regions. On the other hand, a [beta]-turn-motif conserved in archaeal group II chaperonins might facilitate substrate recognition. Our results help us to specify the idea of the open, substrate-accepting state of the thermosome and may provide an additional jigsaw piece in understanding the mode of substrate binding of group II chaperonins. IS - 3 JF - Journal of Molecular Biology EP - 729 TI - NMR Studies on the Substrate-binding Domains of the Thermosome: Structural Plasticity in the Protrusion Region VL - 336 SP - 717 KW - chemical-shift KW - cs-perturbation AU - Heller, Markus AU - John, Michael AU - Coles, Murray AU - Bosch, Gundula AU - Baumeister, Wolfgang AU - Kessler, Horst PY - 2004/02/20/ UR - http://dx.doi.org/10.1016/j.jmb.2003.12.035 ER -