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1999 Crystal structure of gingipain R: anArg-specific bacterial cysteine proteinase with a caspase-like fold Embo J 18 5453 – 5462 . 32

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Acta Biologica Hungarica
Authors: Zoltán Kern, Miklós Kázmér, Tamás Müller, András Specziár, Alexandra Németh, and Tamás Váczi

. 6. Burgess , K. M. N. , Bryce , D. L. ( 2015 ) On the crystal structure of the vaterite polymorph of CaCO 3 : A calcium-43 solid-state NMR and computational assessment . Solid State Nucl. Magn

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17 304 312 Yamashita, A., Singh, S. K., Kawate, T., Jin, Y., Gouaux, E. (2005) Crystal structure of a bacterial homologue of Na + /Cl

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. 223 381 387 Billas, I. M., Moulinier, L., Rochel, N., Moras, D. (2001) Crystal structure of the ligand binding domain of the ultraspiracle protein

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Acta Biologica Hungarica
Authors: J. Kerrigan, C. Ragunath, Lili Kandra, GYöngyi Gyémánt, A. Lipták, L. Jánossy, J. Kaplan, and N. Ramasubbu

, N., Schuette, C. G., Klingenstein, R., Sandhoff, K., Saenger, W. (2003) The X-ray crystal structure of human beta-hexosaminidase B provides new insights into Sandhoff disease. J. Mol. Biol. 328 , 669

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Au, S. W., Leng, X., Harper, J. W., Barford, D. (2002) Implications for the ubiquitination reaction of the anaphase-promoting complex from the crystal structure of the Doc1/Apc10 subunit. J. Mol. Biol. 316

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. , Kakuta , Y. ( 2005 ) Crystal structure of the alginate (poly alpha-L-guluronate) lyase from Corynebacterium sp . at 1.2 A resolution. J. Mol. Biol. 345 , 1111 – 1118 . 17

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. Barden S , Lange S , Tegtmeyer N , Conradi J , Sewald N , Backert S , Niemann HH : A helical RGD motif promoting cell adhesion: crystal structures of the Helicobacter pylori type IV secretion system pilus protein

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European Journal of Microbiology and Immunology
Authors: Manja Boehm, Daniel Simson, Ulrike Escher, Anna-Maria Schmidt, Stefan Bereswill, Nicole Tegtmeyer, Steffen Backert, and Markus M. Heimesaat

. Krojer , T Garrido-Franco , M Huber , R Ehrmann , M Clausen , T . Crystal structure of DegP (HtrA) reveals a new

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Abstract

The crystal structure of the K1 domain, an adhesin module of the lysine gingipain (Kgp) expressed on the cell surface by the periodontopathic anaerobic bacterium, Porphyromonas gingivalis W83, is compared to the previously determined structures of homologues K2 and K3, all three being representative members of the cleaved adhesin domain family. In the structure of K1, the conformation of the most extensive surface loop is unexpectedly perturbed, perhaps by crystal packing, and is displaced from a previously reported arginine-anchored position observed in K2 and K3. This displacement allows the loop to become free to interact with other proteins; the alternate flipped-out loop conformation is a novel mechanism for interacting with target host proteins, other bacteria, or other gingipain protein domains. Further, the K1 adhesin module, like others, is found to be haemolytic in vitro, and so, functions in erythrocyte recognition thereby contributing to the haemolytic function of Kgp. K1 was also observed to selectively bind to haem-albumin with high affinity, suggesting this domain may be involved in gingipain-mediated haem acquisition from haem-albumin. Therefore, it is most likely that all cleaved adhesin domains of Kgp contribute to the pathogenicity of P. gingivalis in more complex ways than simply mediating bacterial adherence.

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