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Quigley, P. M., Korotkov, K., Baneyx, F., Hol, W. G. J. (2003) The 1.6-A crystal structure of the class of chaperones represented by Escherichia coli Hsp31 reveals a putative catalytic triad. Proceedings of the National Academy of Sciences, 100 (6) 3137-3142 doi:10.1073/pnas.0530312100

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Reference TypeJournal (article/letter/editorial)
TitleThe 1.6-A crystal structure of the class of chaperones represented by Escherichia coli Hsp31 reveals a putative catalytic triad
JournalProceedings of the National Academy of Sciences
AuthorsQuigley, P. M.Author
Korotkov, K.Author
Baneyx, F.Author
Hol, W. G. J.Author
Year2003 (March 18)Volume100
Issue6
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.0530312100Search in ResearchGate
Generate Citation Formats
Mindat Ref. ID1693413Long-form Identifiermindat:1:5:1693413:7
GUID0
Full ReferenceQuigley, P. M., Korotkov, K., Baneyx, F., Hol, W. G. J. (2003) The 1.6-A crystal structure of the class of chaperones represented by Escherichia coli Hsp31 reveals a putative catalytic triad. Proceedings of the National Academy of Sciences, 100 (6) 3137-3142 doi:10.1073/pnas.0530312100
Plain TextQuigley, P. M., Korotkov, K., Baneyx, F., Hol, W. G. J. (2003) The 1.6-A crystal structure of the class of chaperones represented by Escherichia coli Hsp31 reveals a putative catalytic triad. Proceedings of the National Academy of Sciences, 100 (6) 3137-3142 doi:10.1073/pnas.0530312100
In(2003, March) Proceedings of the National Academy of Sciences Vol. 100 (6) Proceedings of the National Academy of Sciences

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Sastry, M. S. R., Quigley, P. M., Hol, W. G. J., Baneyx, F. (2004) The linker-loop region of Escherichia coli chaperone Hsp31 functions as a gate that modulates high-affinity substrate binding at elevated temperatures. Proceedings of the National Academy of Sciences, 101 (23) 8587-8592 doi:10.1073/pnas.0403033101
Conroy, M. J., Durand, A., Lupo, D., Li, X.-D., Bullough, P. A., Winkler, F. K., Merrick, M. (2007) The crystal structure of the Escherichia coli AmtB-GlnK complex reveals how GlnK regulates the ammonia channel. Proceedings of the National Academy of Sciences, 104 (4) 1213-1218 doi:10.1073/pnas.0610348104
Ahn, V. E., Faull, K. F., Whitelegge, J. P., Fluharty, A. L., Prive, G. G. (2003) Crystal structure of saposin B reveals a dimeric shell for lipid binding. Proceedings of the National Academy of Sciences, 100 (1) 38-43 doi:10.1073/pnas.0136947100
Dou, F., Netzer, W. J., Tanemura, K., Li, F., Hartl, F. U., Takashima, A., Gouras, G. K., Greengard, P., Xu, H. (2003) Chaperones increase association of tau protein with microtubules. Proceedings of the National Academy of Sciences, 100 (2) 721-726 doi:10.1073/pnas.242720499
Cho, S.-J., Lee, M. G., Yang, J. K., Lee, J. Y., Song, H. K., Suh, S. W. (2000) Crystal structure of Escherichia coli CyaY protein reveals a previously unidentified fold for the evolutionarily conserved frataxin family. Proceedings of the National Academy of Sciences, 97 (16) 8932-8937 doi:10.1073/pnas.160270897
Hakansson, K., Wang, A. H.-J., Miller, C. G. (2000) The structure of aspartyl dipeptidase reveals a unique fold with a Ser-His-Glu catalytic triad. Proceedings of the National Academy of Sciences, 97 (26) 14097-14102 doi:10.1073/pnas.260376797
Bae, W., Xia, B., Inouye, M., Severinov, K. (2000) Escherichia coli CspA-family RNA chaperones are transcription antiterminators. Proceedings of the National Academy of Sciences, 97 (14) 7784-7789 doi:10.1073/pnas.97.14.7784
Alix, J. H., Guerin, M. F. (1993) Mutant DnaK chaperones cause ribosome assembly defects in Escherichia coli. Proceedings of the National Academy of Sciences, 90 (20) 9725-9729 doi:10.1073/pnas.90.20.9725
Vila-Sanjurjo, A., Ridgeway, W. K., Seymaner, V., Zhang, W., Santoso, S., Yu, K., Cate, J. H. D. (2003) X-ray crystal structures of the WT and a hyper-accurate ribosome from Escherichia coli. Proceedings of the National Academy of Sciences, 100 (15) 8682-8687 doi:10.1073/pnas.1133380100
Lobner-Olesen, A., Marinus, M. G., Hansen, F. G. (2003) Role of SeqA and Dam in Escherichia coli gene expression: A global/microarray analysis. Proceedings of the National Academy of Sciences, 100 (8) 4672-4677 doi:10.1073/pnas.0538053100
Chattopadhyay, M. K., Tabor, C. W., Tabor, H. (2003) Polyamines protect Escherichia coli cells from the toxic effect of oxygen. Proceedings of the National Academy of Sciences, 100 (5) 2261-2265 doi:10.1073/pnas.2627990100
 
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