6pev: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==CryoEM Plasmodium falciparum M18 aspartyl aminopeptidase== | |||
<StructureSection load='6pev' size='340' side='right'caption='[[6pev]], [[Resolution|resolution]] 3.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6pev]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Plasmodium_falciparum_(isolate_nf54) Plasmodium falciparum (isolate nf54)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PEV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6PEV FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=6pev FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pev OCA], [http://pdbe.org/6pev PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6pev RCSB], [http://www.ebi.ac.uk/pdbsum/6pev PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6pev ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
X-ray crystallography often requires non-native constructs involving mutations or truncations, and is challenged by membrane proteins and large multicomponent complexes. We present here a bottom-up endogenous structural proteomics approach whereby near-atomic-resolution cryo electron microscopy (cryoEM) maps are reconstructed ab initio from unidentified protein complexes enriched directly from the endogenous cellular milieu, followed by identification and atomic modeling of the proteins. The proteins in each complex are identified using cryoID, a program we developed to identify proteins in ab initio cryoEM maps. As a proof of principle, we applied this approach to the malaria-causing parasite Plasmodium falciparum, an organism that has resisted conventional structural-biology approaches, to obtain atomic models of multiple protein complexes implicated in intraerythrocytic survival of the parasite. Our approach is broadly applicable for determining structures of undiscovered protein complexes enriched directly from endogenous sources. | |||
Bottom-up structural proteomics: cryoEM of protein complexes enriched from the cellular milieu.,Ho CM, Li X, Lai M, Terwilliger TC, Beck JR, Wohlschlegel J, Goldberg DE, Fitzpatrick AWP, Zhou ZH Nat Methods. 2019 Nov 25. pii: 10.1038/s41592-019-0637-y. doi:, 10.1038/s41592-019-0637-y. PMID:31768063<ref>PMID:31768063</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6pev" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Ho, C]] | |||
[[Category: Lai, M]] | |||
[[Category: Zhou, Z H]] | |||
[[Category: Aspartyl aminopeptidase]] | |||
[[Category: Metal binding protein]] | |||
Revision as of 18:11, 11 December 2019
CryoEM Plasmodium falciparum M18 aspartyl aminopeptidaseCryoEM Plasmodium falciparum M18 aspartyl aminopeptidase
Structural highlights
Publication Abstract from PubMedX-ray crystallography often requires non-native constructs involving mutations or truncations, and is challenged by membrane proteins and large multicomponent complexes. We present here a bottom-up endogenous structural proteomics approach whereby near-atomic-resolution cryo electron microscopy (cryoEM) maps are reconstructed ab initio from unidentified protein complexes enriched directly from the endogenous cellular milieu, followed by identification and atomic modeling of the proteins. The proteins in each complex are identified using cryoID, a program we developed to identify proteins in ab initio cryoEM maps. As a proof of principle, we applied this approach to the malaria-causing parasite Plasmodium falciparum, an organism that has resisted conventional structural-biology approaches, to obtain atomic models of multiple protein complexes implicated in intraerythrocytic survival of the parasite. Our approach is broadly applicable for determining structures of undiscovered protein complexes enriched directly from endogenous sources. Bottom-up structural proteomics: cryoEM of protein complexes enriched from the cellular milieu.,Ho CM, Li X, Lai M, Terwilliger TC, Beck JR, Wohlschlegel J, Goldberg DE, Fitzpatrick AWP, Zhou ZH Nat Methods. 2019 Nov 25. pii: 10.1038/s41592-019-0637-y. doi:, 10.1038/s41592-019-0637-y. PMID:31768063[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||