4eyy: Difference between revisions
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==Crystal Structure of the IcmR-IcmQ complex from Legionella pneumophila== | |||
<StructureSection load='4eyy' size='340' side='right' caption='[[4eyy]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4eyy]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Legpc Legpc] and [http://en.wikipedia.org/wiki/Legph Legph]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EYY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EYY FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3fxd|3fxd]], [[3fxe|3fxe]]</td></tr> | |||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">icmR, lpg0443 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272624 LEGPH]), icmQ, LPC_2899 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=400673 LEGPC])</td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4eyy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eyy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4eyy RCSB], [http://www.ebi.ac.uk/pdbsum/4eyy PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== 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> | |||
[[Category: | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
[[Category: | </div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Legpc]] | |||
[[Category: Legph]] | |||
[[Category: Akey, C W.]] | [[Category: Akey, C W.]] | ||
[[Category: Akey, I V.]] | [[Category: Akey, I V.]] | ||
Revision as of 09:10, 16 July 2014
Crystal Structure of the IcmR-IcmQ complex from Legionella pneumophila
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