This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
5xfs
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<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]] | ||
Revision as of 07:55, 6 December 2017
Crystal structure of PE8-PPE15 in complex with EspG5 from M. tuberculosis
| |||||||||||
