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International Institute of Molecular and Cell Biology Warsaw, Poland

Laboratory of Structural Biology Max-Planck-PAN Joint Junior Research Group. Max-Planck Institute of Molecular Cell Biology and Genetics Dresden, Germany. International Institute of Molecular and Cell Biology Warsaw, Poland. Physics in Biology: Protein Crystallography.

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International Institute of Molecular and Cell Biology Warsaw, Poland

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  1. Laboratory of Structural Biology Max-Planck-PAN Joint Junior Research Group Max-Planck Institute of Molecular Cell Biology and Genetics Dresden, Germany International Institute of Molecular and Cell Biology Warsaw, Poland Physics in Biology: Protein Crystallography

  2. From physics to biology Crystallography of sapphire Walther group, Munich Protein crystallography Warsaw

  3. Crystallography shows tremendous complexity at high magnification. 108 10-8 10

  4. Bacterial cell walls membrane peptidoglycan peptidoglycan membrane membrane Gram negative Gram positive Peptidoglycan detail

  5. N-domain catalytic domain C-domain lysostaphin HxH LytM HxH LytM was studied as a model system for lysostaphin.

  6. LytM is a new fold in proteolysis Zinc ligands: H 210 D 214 H 293 Occluding ligand: N117 N-domain C-domain S. G. Odintsov, I. Sabala, M. Marcyjaniak, and M. Bochtler, Latent LytM at 1.3A resolution. J Mol Biol, 2004. 335(3): p. 775-85.

  7. Unexpected local similarities LytM, mature form D-Ala-D-Ala carboxypeptidase Sonic hedgehog, N-domain Bochtler M, Odintsov SG, Marcyjaniak M, Sabala I. Similar active sites in lysostaphins and D-Ala-D-Ala metallopeptidases. Protein Sci. 2004 13 (4): p. 854-61.

  8. MepA-type enzymes could be LAS enzymes. HX3-6D HXH

  9. Summary: the LAS group so far LytM (active form) MepA D-Ala-D-Ala carboxypeptidase VanX Sonic hedgehog N-domain

  10. Another unknown peptidoglycan amidase, unknown fold and function blue highest conservation, red lowest conservation Korza HJ, Bochtler M. P. aeruginosa LD-carboxypeptidase: A serine peptidase with a Ser-His-Glu triad and a nucleophilic elbow. J Biol Chem. 2005 Sep 14; [Epub ahead of print]

  11. A serine peptidase with a Ser-His-Glu triad. Note that mutated enzymes were used in 100-fold higher concentration and incubated longer than wild-type enzyme to make the comparison more stringent.

  12. The active site serines are Ramachandran outliers.

  13. LD-carboxypeptidase -hydrolase (in this case, a lipase)

  14. Acknowledgement:

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