5xfs: Difference between revisions

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 ==Crystal structure of PE8-PPE15 in complex with EspG5 from M. tuberculosis==
-<StructureSection load='5xfs' size='340' side='right' caption='[[5xfs]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
+<StructureSection load='5xfs' size='340' side='right'caption='[[5xfs]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5xfs]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XFS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XFS FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5xfs]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XFS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XFS FirstGlance]. <br>
-</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=5xfs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xfs OCA], [http://pdbe.org/5xfs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xfs RCSB], [http://www.ebi.ac.uk/pdbsum/5xfs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xfs ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</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=5xfs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xfs OCA], [https://pdbe.org/5xfs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xfs RCSB], [https://www.ebi.ac.uk/pdbsum/5xfs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xfs ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ESPG5_MYCTU ESPG5_MYCTU]] Specific chaperone for cognate PE/PPE proteins. Plays an important role in preventing aggregation of PE/PPE dimers.<ref>PMID:25155747</ref>  [[http://www.uniprot.org/uniprot/PPE15_MYCTU PPE15_MYCTU]] May play a critical role in the homeostasis of triacylglycerol-containing lipid droplets in M.tuberculosis and influence the entry of the pathogen into a dormant state.<ref>PMID:27325376</ref>
+[https://www.uniprot.org/uniprot/L7N667_MYCTU L7N667_MYCTU]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Mycobacterium tuberculosis (Mtb), the causative agent of tuberculosis, has developed multiple strategies to adapt to the human host. The five type VII secretion systems, ESX-1-5, direct the export of many virulence-promoting protein effectors across the complex mycobacterial cell wall. One class of ESX substrates is the PE-PPE family of proteins, which is unique to mycobacteria and essential for infection, antigenic variation, and host-pathogen interactions. The genome of Mtb encodes 168 PE-PPE proteins. Many of them are thought to be secreted through ESX-5 secretion system and to function in pairs. However, understanding of the specific pairing of PE-PPE proteins and their structure-function relationship is limited by the challenging purification of many PE-PPE proteins, and our knowledge of the PE-PPE interactions therefore has been restricted to the PE25-PPE41 pair and its complex with the ESX-5 secretion system chaperone EspG5. Here, we report the crystal structure of a new PE-PPE pair, PE8-PPE15, in complex with EspG5. Our structure revealed that the EspG5-binding sites on PPE15 are relatively conserved among Mtb PPE proteins, suggesting that EspG5-PPE15 represents a more typical model for EspG5-PPE interactions than EspG5-PPE41. A structural comparison with the PE25-PPE41 complex disclosed conformational changes in the four-helix bundle structure and a unique binding mode in the PE8-PPE15 pair. Moreover, homology-modeling and mutagenesis studies further delineated the molecular determinants of the specific PE-PPE interactions. These findings help develop an atomic algorithm of ESX-5 substrate recognition and PE-PPE pairing.
+Structural basis of the PE-PPE protein interaction in Mycobacterium tuberculosis.,Chen X, Cheng HF, Zhou J, Chan CY, Lau KF, Tsui SK, Au SW J Biol Chem. 2017 Oct 13;292(41):16880-16890. doi: 10.1074/jbc.M117.802645. Epub , 2017 Aug 23. PMID:28842489<ref>PMID:28842489</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 5xfs" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Au, S W.N]]
+[[Category: Large Structures]]
-[[Category: Chen, X]]
+[[Category: Mycobacterium tuberculosis H37Rv]]
-[[Category: Bacterial pathogenesis]]
+[[Category: Au SWN]]
-[[Category: Protein complex]]
+[[Category: Chen X]]
-[[Category: Protein secretion]]
-[[Category: Protein structure]]
-[[Category: Protein transport]]
-[[Category: Tuberculosis]]