4eyy

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4eyy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eyy OCA], [https://pdbe.org/4eyy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eyy RCSB], [https://www.ebi.ac.uk/pdbsum/4eyy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eyy ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

A Type 4b secretion system (T4bSS) is required for Legionella growth in alveolar macrophages. IcmQ associates with IcmR, binds to membranes, and has a critical role in the T4bSS. We have now solved a crystal structure of IcmR-IcmQ to further our understanding of this complex. This structure revealed an amphipathic four-helix bundle, formed by IcmR and the N-terminal domain of IcmQ, which is linked to a novel C-terminal domain of IcmQ (Qc) by a linker helix. The Qc domain has structural homology with ADP ribosyltransferase domains in certain bacterial toxins and binds NAD(+) with a dissociation constant in the physiological range. Structural homology and molecular dynamics were used to identify an extended NAD(+) binding site on Qc, and the resulting model was tested by mutagenesis and binding assays. Based on the data, we suggest that IcmR-IcmQ binds to membranes, where it may interact with, or perhaps modify, a protein in the T4bSS when NAD(+) is bound.

IcmQ in the Type 4b secretion system contains an NAD+ binding domain.,Farelli JD, Gumbart JC, Akey IV, Hempstead A, Amyot W, Head JF, McKnight CJ, Isberg RR, Akey CW Structure. 2013 Aug 6;21(8):1361-73. doi: 10.1016/j.str.2013.05.017. Epub 2013, Jul 11. PMID:23850453<ref>PMID:23850453</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

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