5i1t

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5i1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i1t OCA], [http://pdbe.org/5i1t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5i1t RCSB], [http://www.ebi.ac.uk/pdbsum/5i1t PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5i1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i1t OCA], [http://pdbe.org/5i1t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5i1t RCSB], [http://www.ebi.ac.uk/pdbsum/5i1t PDBsum]</span></td></tr>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Bacterial spores are the most resistant form of life known on the Earth and represent a serious problem for i) bioterrorism attack, ii) horizontal transmission of microbial pathogens in the community and iii) persistence in patients and in a nosocomial environment. SpoIID (Stage II Sporulation Protein D) is a Lytic Transglycosylase (LT) essential for sporulation. The LT-superfamily is a potential drug target because they are active in essential bacterial processes involving the peptidoglycan (PGN), which is unique to bacteria. However, the absence of structural information for the sporulation specific LT enzymes has hindered mechanistic understanding of SpoIID. Here, we report the first crystal structures with and without ligands of the SpoIID family from two community relevant spore-forming pathogens, Bacillus anthracis and Clostridium difficile. The structures allow us to visualize the overall architecture, characterize the substrate recognition model, identify critical residues and provide the structural basis for catalysis by this new family of enzymes.
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Crystal structures of the SpoIID lytic transglycosylases essential for bacterial sporulation.,Nocadello S, Minasov G, Shuvalova LS, Dubrovska I, Sabini E, Anderson WF J Biol Chem. 2016 May 18. pii: jbc.M116.729749. PMID:27226615<ref>PMID:27226615</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5i1t" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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Revision as of 07:29, 20 June 2016

2.6 Angstrom Resolution Crystal Structure of Stage II Sporulation Protein D (SpoIID) from Clostridium difficile in Complex with Triacetylchitotriose

5i1t, resolution 2.60Å

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