X-ray sequence and crystal structure of luffaculin 1, a novel type 1 ribosome-inactivating protein-5

<p><b>Copyright information:</b></p><p>Taken from "X-ray sequence and crystal structure of luffaculin 1, a novel type 1 ribosome-inactivating protein"</p><p>http://www.biomedcentral.com/1472-6807/7/29</p><p>BMC Structural Biology 2007;7():29-29.</p><p>Published online 30 Apr 2007</p><p>PMCID:PMC1868734.</p><p></p>ellow, respectively

X-ray sequence and crystal structure of luffaculin 1, a novel type 1 ribosome-inactivating protein-1

<p><b>Copyright information:</b></p><p>Taken from "X-ray sequence and crystal structure of luffaculin 1, a novel type 1 ribosome-inactivating protein"</p><p>http://www.biomedcentral.com/1472-6807/7/29</p><p>BMC Structural Biology 2007;7():29-29.</p><p>Published online 30 Apr 2007</p><p>PMCID:PMC1868734.</p><p></p>tlined in the boxes

X-ray sequence and crystal structure of luffaculin 1, a novel type 1 ribosome-inactivating protein-4

<p><b>Copyright information:</b></p><p>Taken from "X-ray sequence and crystal structure of luffaculin 1, a novel type 1 ribosome-inactivating protein"</p><p>http://www.biomedcentral.com/1472-6807/7/29</p><p>BMC Structural Biology 2007;7():29-29.</p><p>Published online 30 Apr 2007</p><p>PMCID:PMC1868734.</p><p></p>s with numbers denoting the respective distances in the unit of Å. (a) shows that Asp65 of molecule A has hydrogen bond interaction with Thr67 and salt bridge with Arg46 besides interaction with water molecules S244 and S265. (b) shows that Val212 of molecule A resides in a hydrophobic environment. (c) shows that Gln220 of molecule A has no interaction with other residues except the hydrogen bond with the symmetry related water molecule S327

X-ray sequence and crystal structure of luffaculin 1, a novel type 1 ribosome-inactivating protein-2

<p><b>Copyright information:</b></p><p>Taken from "X-ray sequence and crystal structure of luffaculin 1, a novel type 1 ribosome-inactivating protein"</p><p>http://www.biomedcentral.com/1472-6807/7/29</p><p>BMC Structural Biology 2007;7():29-29.</p><p>Published online 30 Apr 2007</p><p>PMCID:PMC1868734.</p><p></p> are different from luffin a. (b) shows residues 46, 94 and 129 with clear electron density in molecule A and B contoured at 2σ. (c) shows residue 185 with weak electron density in molecule B can be clearly recognized as Ile in the electron density of molecule A

X-ray sequence and crystal structure of luffaculin 1, a novel type 1 ribosome-inactivating protein-6

<p><b>Copyright information:</b></p><p>Taken from "X-ray sequence and crystal structure of luffaculin 1, a novel type 1 ribosome-inactivating protein"</p><p>http://www.biomedcentral.com/1472-6807/7/29</p><p>BMC Structural Biology 2007;7():29-29.</p><p>Published online 30 Apr 2007</p><p>PMCID:PMC1868734.</p><p></p> boxes A and B, respectively. The largest deviation region at the β8-strand of the N-terminal region is outlined in the box C

X-ray sequence and crystal structure of luffaculin 1, a novel type 1 ribosome-inactivating protein-0

<p><b>Copyright information:</b></p><p>Taken from "X-ray sequence and crystal structure of luffaculin 1, a novel type 1 ribosome-inactivating protein"</p><p>http://www.biomedcentral.com/1472-6807/7/29</p><p>BMC Structural Biology 2007;7():29-29.</p><p>Published online 30 Apr 2007</p><p>PMCID:PMC1868734.</p><p></p>sentations are residues Tyr70, Tyr110, Glu159 and Arg162 in the active site, and the two N-acetylglucosamines that are each covalently linked to Asn 77 and 84, respectively. All figures except for Fig. 4 were prepared using Pymol [46]