Comparative structural analysis of psychrophilic and meso- and thermophilic enzymes.

@article{citeulike:2288237, abstract = {Enzymes adapted to cold display structures comparable with those of their meso- and thermophilic homologs but are characterized by a higher catalytic efficiency at low temperatures and by thermolability at moderate temperatures. To identify the structural factors responsible of such features, we undertook a systematic comparative analysis of several structural properties in a data set consisting of 7 cold active enzymes belonging to different structural families and 28 related structures from meso/thermophiles representing most of the structural information now available. Only high-resolution and high-quality structures were considered. Properties were calculated and then compared for each pair of 3D structures displaying different temperatures of adaptation using a temperature-weighting scheme. The significance of the resulting differences was evaluated with a statistical method. Results reveal that each protein family adopts different structural strategies to adapt to low temperatures. However, some common trends are observed: the number of ion pairs, the side-chain contribution to the exposed surface, and the apolar fraction of the buried surface show a consistent decrease with decreasing optimal temperatures.}, address = {Dipartimento di Scienze Biochimiche, A. Rossi Fanelli, and Centro di Biologia Molecolare del C.N.R., Universit\`{a} La Sapienza, Roma, Italy.}, author = {Gianese, G. and Bossa, F. and Pascarella, S. }, citeulike-article-id = {2288237}, issn = {1097-0134}, journal = {Proteins}, keywords = {enzyme, for-thuber, mesophily, protein, psychrophily, structure, thermal, thermophily}, month = {May}, number = {2}, pages = {236--249}, posted-at = {2008-01-25 06:33:18}, priority = {2}, title = {Comparative structural analysis of psychrophilic and meso- and thermophilic enzymes.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/11933070}, volume = {47}, year = {2002} }

TY - JOUR ID - citeulike:2288237 L3 - citeulike-article-id:2288237 TI - Comparative structural analysis of psychrophilic and meso- and thermophilic enzymes. JF - Proteins VL - 47 IS - 2 SP - 236 EP - 249 AD - Dipartimento di Scienze Biochimiche, A. Rossi Fanelli, and Centro di Biologia Molecolare del C.N.R., Università La Sapienza, Roma, Italy. SN - 1097-0134 N2 - Enzymes adapted to cold display structures comparable with those of their meso- and thermophilic homologs but are characterized by a higher catalytic efficiency at low temperatures and by thermolability at moderate temperatures. To identify the structural factors responsible of such features, we undertook a systematic comparative analysis of several structural properties in a data set consisting of 7 cold active enzymes belonging to different structural families and 28 related structures from meso/thermophiles representing most of the structural information now available. Only high-resolution and high-quality structures were considered. Properties were calculated and then compared for each pair of 3D structures displaying different temperatures of adaptation using a temperature-weighting scheme. The significance of the resulting differences was evaluated with a statistical method. Results reveal that each protein family adopts different structural strategies to adapt to low temperatures. However, some common trends are observed: the number of ion pairs, the side-chain contribution to the exposed surface, and the apolar fraction of the buried surface show a consistent decrease with decreasing optimal temperatures. KW - enzyme KW - for-thuber KW - mesophily KW - protein KW - psychrophily KW - structure KW - thermal KW - thermophily AU - Gianese, G AU - Bossa, F AU - Pascarella, S PY - 2002/05/01/ UR - http://view.ncbi.nlm.nih.gov/pubmed/11933070 ER -