|
|
| (2 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==Crystal structure of Pf12 tandem 6-cys domains from Plasmodium falciparum== | | ==Crystal structure of Pf12 tandem 6-cys domains from Plasmodium falciparum== |
| - | <StructureSection load='2ymo' size='340' side='right' caption='[[2ymo]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='2ymo' size='340' side='right'caption='[[2ymo]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ymo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Plaf7 Plaf7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YMO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YMO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ymo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum_3D7 Plasmodium falciparum 3D7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YMO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YMO 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=2ymo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ymo OCA], [http://pdbe.org/2ymo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ymo RCSB], [http://www.ebi.ac.uk/pdbsum/2ymo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ymo 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]] 1.9Å</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=2ymo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ymo OCA], [https://pdbe.org/2ymo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ymo RCSB], [https://www.ebi.ac.uk/pdbsum/2ymo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ymo ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/PF12_PLAF7 PF12_PLAF7] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 19: |
Line 22: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Plaf7]] | + | [[Category: Large Structures]] |
| - | [[Category: Arredondo, S A]] | + | [[Category: Plasmodium falciparum 3D7]] |
| - | [[Category: Boulanger, M J]] | + | [[Category: Arredondo SA]] |
| - | [[Category: Grigg, M E]] | + | [[Category: Boulanger MJ]] |
| - | [[Category: Loveless, B C]] | + | [[Category: Grigg ME]] |
| - | [[Category: Miller, L H]] | + | [[Category: Loveless BC]] |
| - | [[Category: Tonkin, M L]] | + | [[Category: Miller LH]] |
| - | [[Category: 6-cysteine]] | + | [[Category: Tonkin ML]] |
| - | [[Category: Apicomplexa]]
| + | |
| - | [[Category: Blood stage antigen]]
| + | |
| - | [[Category: Malaria]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Vaccine]]
| + | |
| Structural highlights
Function
PF12_PLAF7
Publication Abstract from PubMed
Plasmodium falciparum is the most devastating agent of human malaria. A major contributor to its virulence is a complex lifecycle with multiple parasite forms, each presenting a different repertoire of surface antigens. Importantly, members of the 6-Cys s48/45 family of proteins are found on the surface of P. falciparum in every stage and several of these antigens have been investigated as vaccine targets. Pf12 is the archetypal member of the 6-Cys protein family, containing just two s48/45 domains, while other members have up to fourteen of these domains. Pf12 is strongly recognized by immune sera from naturally infected patients. Here we show that Pf12 is highly conserved and under purifying selection. Immunofluorescence data reveals a punctate staining pattern with an apical organization in late schizonts. Together, these data are consistent with an important functional role for Pf12 in parasite-host cell attachment or invasion. To infer the structural and functional diversity between Pf12 and the other eleven 6-Cys domain proteins, we solved the 1.90 A resolution crystal structure of the Pf12 ectodomain. Structural analysis reveals a unique organization between the membrane proximal and membrane distal domains and clear homology with the SRS-domain containing proteins of Toxoplasma gondii. Crosslinking and mass spectrometry confirm the previously identified Pf12-Pf41 heterodimeric complex, and analysis of individual crosslinks supports an unexpected antiparallel organization. Collectively, the localization and structure of Pf12 and details of its interaction with Pf41 reveal important insight into the structural and functional properties of this archetypal member of the 6-Cys protein family.
Structural and biochemical characterization of Plasmodium falciparum 12 (Pf12) reveals a unique inter-domain organization and the potential for an antiparallel arrangement with Pf41.,Tonkin ML, Arredondo SA, Loveless BC, Serpa JJ, Makepeace KA, Sundar N, Petrotchenko EV, Miller LH, Grigg ME, Boulanger MJ J Biol Chem. 2013 Mar 19. PMID:23511632[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tonkin ML, Arredondo SA, Loveless BC, Serpa JJ, Makepeace KA, Sundar N, Petrotchenko EV, Miller LH, Grigg ME, Boulanger MJ. Structural and biochemical characterization of Plasmodium falciparum 12 (Pf12) reveals a unique inter-domain organization and the potential for an antiparallel arrangement with Pf41. J Biol Chem. 2013 Mar 19. PMID:23511632 doi:10.1074/jbc.M113.455667
|
