I feel compelled to throw a few references into the ring.
NFAT is a protein where you get a good sampling of snapshots: 1. Folded up as a monomer when interacting with partner proteins: http://www.ncbi.nlm.nih.gov/pubmed/9510247 http://www.ncbi.nlm.nih.gov/pubmed/16873067 2. Extended as a dimer: http://www.ncbi.nlm.nih.gov/pubmed/12949493 3. Folded up as a monomer when interacting with a partner protein which happens to be itself as an extended dimer: http://www.ncbi.nlm.nih.gov/pubmed/18462673 4. Wrapped around DNA as a monomer without partners:. http://www.ncbi.nlm.nih.gov/pubmed/14643663 In this last reference you get a sample of extended, wrapped around, and folded up all in the same unit cell! James On Feb 15, 2012, at 1:48 PM, Jacob Keller wrote: > Dear Crystallographers, > > thanks for all of the responses and conversation. I have culled > together the various references which have been sent on the BB and > which I have come up with, and posted them below. Worthy of special > mention, I think, is the first one (Lange et al), in which 46 (!) > different crystal structures are pitted against a lot of RDC NMR data, > and the match seems to be excellent (although it seems you probably > have to know both methods fairly well to evaluate this properly.) > Anyway, for asserting that variances between crystal structures at > least in some cases represent differences between > physiologically-relevant states in solution, the Lange paper is really > on the mark. > > Thanks again, > > Jacob > > Lange OF, Lakomek NA, Farès C, Schröder GF, Walter KF, Becker S, > Meiler J, Grubmüller H, Griesinger C, de Groot BL. > Recognition dynamics up to microseconds revealed from an RDC-derived > ubiquitin ensemble in solution. > Science. 2008 Jun 13;320(5882):1471-5. PubMed PMID: 18556554. > > > Kondrashov, D.A., Zhang, W., Aranda, R.t., Stec, B., and Phillips, > G.N., Jr. (2008). Sampling of the native conformational ensemble of > myoglobin via structures in different crystalline environments. > Proteins 70, 353-362. > > Zhang, X. J., Wozniak, J. A., and Matthews, B. W. (1995) Protein > flexibility and adaptability seen in 25 crystal forms of T4 lysozyme, > Journal of molecular biology 250, 527-552. > > Long, SB, Casey, P., Beese, LS (2002) The reaction path of protein > farnesyltransferase at atomic resolution. Nature Oct 10; > 419(6907):645-50. > http://www.ncbi.nlm.nih.gov/pubmed?term=The%20reaction%20path%20of%20protein%20farnesyltransferase%20at%20atomic%20resolution > > J. R. Kiefer, C. Mao, J. C. Braman and L. S. Beese (1998) “Visualizing > DNA replication in a catalytically active Bacillus DNA polymerase > crystal” Nature 6664:304-7. > http://www.ncbi.nlm.nih.gov/pubmed?term=Visualizing%20DNA%20replication%20in%20a%20catalytically%20active%20Bacillus%20DNA%20polymerase%20crystal > > Mancini EJ, Kainov DE, Grimes JM, Tuma R, Bamford DH, Stuart DI (2004) > "Atomic snapshots of an RNA packaging motor reveal conformational > changes linking ATP hydrolysis to RNA translocation." > Cell 118(6):743-55 > http://www.cell.com/abstract/S0092-8674(04)00837-2 > > Nature. 2009 Dec 3;462(7273):669-73. > Hidden alternative structures of proline isomerase essential for catalysis. > Fraser JS, Clarkson MW, Degnan SC, Erion R, Kern D, Alber T. > > > > > ******************************************* > Jacob Pearson Keller > Northwestern University > Medical Scientist Training Program > email: j-kell...@northwestern.edu > *******************************************
