5xfs: Difference between revisions
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<StructureSection load='5xfs' size='340' side='right' caption='[[5xfs]], [[Resolution|resolution]] 2.90Å' scene=''> | <StructureSection load='5xfs' size='340' side='right' caption='[[5xfs]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
== Structural highlights == | == 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 [http://en.wikipedia.org/wiki/Myctu Myctu]. 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> | ||
</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PE8, Rv1040c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU]), PPE15, mper1, Rv1039c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU]), espG5, Rv1794, LH57_09810 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</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> | |||
</table> | </table> | ||
== Function == | == 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> | [[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> | ||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5xfs" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Myctu]] | |||
[[Category: Au, S W.N]] | [[Category: Au, S W.N]] | ||
[[Category: Chen, X]] | [[Category: Chen, X]] | ||