Crystal Structure of Thermus aquaticus Core RNA Polymerase at 3.3 A Resolution

by: Gongyi Zhang, Elizabeth A Campbell, Leonid Minakhin, Catherine Richter, Konstantin Severinov, Seth A Darst

Cell, Vol. 98, No. 6. (17 September 1999), pp. 811-824.

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Abstract

The X-ray crystal structure of Thermus aquaticus core RNA polymerase reveals a "crab claw"-shaped molecule with a 27 A wide internal channel. Located on the back wall of the channel is a Mg2+ ion required for catalytic activity, which is chelated by an absolutely conserved motif from all bacterial and eukaryotic cellular RNA polymerases. The structure places key functional sites, defined by mutational and cross-linking analysis, on the inner walls of the channel in close proximity to the active center Mg2+. Further out from the catalytic center, structural features are found that may be involved in maintaining the melted transcription bubble, clamping onto the RNA product and/or DNA template to assure processivity, and delivering nucleotide substrates to the active center.

@article{zhang1999, abstract = {The X-ray crystal structure of Thermus aquaticus core RNA polymerase reveals a "crab claw"-shaped molecule with a 27 A wide internal channel. Located on the back wall of the channel is a Mg2+ ion required for catalytic activity, which is chelated by an absolutely conserved motif from all bacterial and eukaryotic cellular RNA polymerases. The structure places key functional sites, defined by mutational and cross-linking analysis, on the inner walls of the channel in close proximity to the active center Mg2+. Further out from the catalytic center, structural features are found that may be involved in maintaining the melted transcription bubble, clamping onto the RNA product and/or DNA template to assure processivity, and delivering nucleotide substrates to the active center.}, author = {Zhang, Gongyi and Campbell, Elizabeth A. and Minakhin, Leonid and Richter, Catherine and Severinov, Konstantin and Darst, Seth A. }, citeulike-article-id = {2646549}, doi = {http://dx.doi.org/10.1016/S0092-8674(00)81515-9}, journal = {Cell}, keywords = {chapter, ppi, xray}, month = {September}, number = {6}, pages = {811--824}, posted-at = {2008-04-09 18:05:15}, priority = {2}, title = {Crystal Structure of Thermus aquaticus Core RNA Polymerase at 3.3 A Resolution}, url = {http://dx.doi.org/10.1016/S0092-8674(00)81515-9}, volume = {98}, year = {1999} }

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TY - JOUR ID - zhang1999 L3 - citeulike-article-id:2646549 TI - Crystal Structure of Thermus aquaticus Core RNA Polymerase at 3.3 A Resolution JF - Cell VL - 98 IS - 6 SP - 811 EP - 824 N2 - The X-ray crystal structure of Thermus aquaticus core RNA polymerase reveals a "crab claw"-shaped molecule with a 27 A wide internal channel. Located on the back wall of the channel is a Mg2+ ion required for catalytic activity, which is chelated by an absolutely conserved motif from all bacterial and eukaryotic cellular RNA polymerases. The structure places key functional sites, defined by mutational and cross-linking analysis, on the inner walls of the channel in close proximity to the active center Mg2+. Further out from the catalytic center, structural features are found that may be involved in maintaining the melted transcription bubble, clamping onto the RNA product and/or DNA template to assure processivity, and delivering nucleotide substrates to the active center. KW - chapter KW - ppi KW - xray AU - Zhang, Gongyi AU - Campbell, Elizabeth AU - Minakhin, Leonid AU - Richter, Catherine AU - Severinov, Konstantin AU - Darst, Seth PY - 1999/09/17/ UR - http://dx.doi.org/10.1016/S0092-8674(00)81515-9 ER -

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