Molecular mechanisms for multitasking: recent crystal structures of moonlighting proteins.

@article{citeulike:527204, abstract = {Recently determined X-ray crystal structures of moonlighting proteins are helping to elucidate how a protein can evolve two different functions and, in some cases, switch between its two functions in response to cellular conditions. X-ray crystal structures of the I-AniI homing endonuclease/maturase and the PutA proline dehydrogenase/transcription factor have provided evidence that these proteins utilize separate protein surfaces for their multiple functions. Also, the structure of the DegP (HtrA) protease/chaperone has revealed information about the mechanism of its chaperone activity and suggests how the protein regulates its protease activity. Comparing the structure of eta-crystallin/retinal dehydrogenase with structures of its single-function enzyme homologs provides clues to changes in the protein structure that may have improved its ability to serve as a crystallin, but at the same time may have adversely affected its catalytic activity.}, address = {Laboratory for Molecular Biology, Department of Biological Sciences, MC567, University of Illinois at Chicago, 900 South Ashland Avenue, Chicago, Illinois 60607, USA.}, author = {Jeffery, C. J. }, citeulike-article-id = {527204}, doi = {http://dx.doi.org/10.1016/j.sbi.2004.10.001}, issn = {0959-440X}, journal = {Curr Opin Struct Biol}, keywords = {enzyme, moonlighting\_enzyme, review, structure}, month = {December}, number = {6}, pages = {663--668}, posted-at = {2007-04-16 03:30:45}, priority = {2}, title = {Molecular mechanisms for multitasking: recent crystal structures of moonlighting proteins.}, url = {http://dx.doi.org/10.1016/j.sbi.2004.10.001}, volume = {14}, year = {2004} }

TY - JOUR ID - citeulike:527204 L3 - citeulike-article-id:527204 TI - Molecular mechanisms for multitasking: recent crystal structures of moonlighting proteins. JF - Curr Opin Struct Biol VL - 14 IS - 6 SP - 663 EP - 668 AD - Laboratory for Molecular Biology, Department of Biological Sciences, MC567, University of Illinois at Chicago, 900 South Ashland Avenue, Chicago, Illinois 60607, USA. SN - 0959-440X N2 - Recently determined X-ray crystal structures of moonlighting proteins are helping to elucidate how a protein can evolve two different functions and, in some cases, switch between its two functions in response to cellular conditions. X-ray crystal structures of the I-AniI homing endonuclease/maturase and the PutA proline dehydrogenase/transcription factor have provided evidence that these proteins utilize separate protein surfaces for their multiple functions. Also, the structure of the DegP (HtrA) protease/chaperone has revealed information about the mechanism of its chaperone activity and suggests how the protein regulates its protease activity. Comparing the structure of eta-crystallin/retinal dehydrogenase with structures of its single-function enzyme homologs provides clues to changes in the protein structure that may have improved its ability to serve as a crystallin, but at the same time may have adversely affected its catalytic activity. KW - enzyme KW - moonlighting_enzyme KW - review KW - structure AU - Jeffery, CJ PY - 2004/12// UR - http://dx.doi.org/10.1016/j.sbi.2004.10.001 ER -