@article {2072,
	title = {Phage display and crystallographic analysis reveals potential substrate/binding site interactions in the protein secretion chaperone CsaA from Agrobacterium tumefaciens},
	journal = {Journal of Molecular Biology},
	volume = {379},
	number = {3},
	year = {2008},
	note = {ISI Document Delivery No.: 311FQTimes Cited: 0Cited Reference Count: 52Feldman, Anat R. Shapova, Yuliya A. Wu, Sampson S. T. Oliver, David C. Heller, Markus McIntosh, Lawrence P. Scott, Jamie K. Paetzel, Mark},
	month = {Jun},
	pages = {457-470},
	type = {Article},
	abstract = {The protein CsaA has been proposed to function as a protein secretion chaperone in bacteria that lack the Sec-dependent protein-targeting chaperone SecB. CsaA is a homodimer with two putative substrate-binding pockets, one in each monomer. To test the hypothesis that these cavities are indeed substrate-binding sites able to interact with other polypeptide chains, we selected a peptide that bound to CsaA from a random peptide library displayed on phage. Presented here is the structure of CsaA from Agrobacterium tumefaciens (AtCsaA) solved in the presence and absence of the selected peptide. To promote co-crystallization, the sequence for this peptide was genetically fused to the amino-terminus of AtCsaA. The resulting 1.65 angstrom resolution crystal structure reveals that the tethered peptide from one AtCsaA molecule binds to the proposed substrate-binding pocket of a symmetry-related molecule possibly mimicking the interaction between a pre-protein substrate and CsaA. The structure shows that the peptide lies in an extended conformation with alanine, proline and glutamine side chains pointing into the binding pocket. The peptide interacts with the atoms of the AtCsaA-binding pocket via seven direct hydrogen bonds. The side chain of a conserved pocket residue, Arg76, has an "up" conformation when the CsaA-binding site is empty and a "down" conformation when the CsaA-binding site is occupied, suggesting that this residue may function to stabilize the peptide in the binding cavity. The presented aggregation assays, phage-display analysis and structural analysis are consistent with AtCsaA being a general chaperone. The properties of the proposed CsaA-binding pocket/peptide interactions are compared to those from other structurally characterized molecular chaperones. (c) 2008 Elsevier Ltd. All rights reserved.},
	keywords = {BACILLUS-SUBTILIS CSAA, BACTERIAL SIGNAL PEPTIDASE, BINDING PROTEIN, CHANNEL, CRYSTAL-STRUCTURE, CsaA, DISPLAY, LIBRARIES, molecular chaperone, phage, PROTEIN SECRETION, protein targeting, SECA, SEQUENCE, STRUCTURAL SUPERPOSITION, TRANSLOCATION},
	isbn = {0022-2836},
	url = {<Go to ISI>://000256586500006},
	author = {Feldman, A. R. and Shapova, Y. A. and Wu, S. S. T. and Oliver, D. C. and Heller, M. and McIntosh, L. P. and Scott, J. K. and Paetzel, M.}
}
@article {1463,
	title = {Caminosides B-D, antimicrobial glycolipids isolated from the marine sponge Caminus sphaeroconia},
	journal = {Journal of Natural Products},
	volume = {69},
	number = {2},
	year = {2006},
	note = {ISI Document Delivery No.: 020WHTimes Cited: 9Cited Reference Count: 10},
	month = {Feb},
	pages = {173-177},
	type = {Article},
	abstract = {A screening pro-rain aimed at discovering inhibitors of the bacterial type III secretion system identified the MeOH extract of the Caribbean sponge Caminus sphaeroconia as an active hit in the initial assay. Bioassay-guided fractionation of the crude extract. led to the isolation of caminosides A (1) to D (4), a family of antimicrobial glycolipids. The structures of the three new caminosides B (2) to D (4) have been elucidated by spectroscopic analysis.},
	keywords = {PROTEIN SECRETION, SYSTEMS},
	isbn = {0163-3864},
	url = {<Go to ISI>://000235943400001},
	author = {Linington, R. G. and Robertson, M. and Gauthier, A. and Finlay, B. B. and MacMillan, J. B. and Molinski, T. F. and Van Soest, R. and Andersen, R. J.}
}
