5lnc
From Proteopedia
(Difference between revisions)
m (Protected "5lnc" [edit=sysop:move=sysop]) |
|||
Line 1: | Line 1: | ||
- | '''Unreleased structure''' | ||
- | + | ==Structure of SPX domain of the yeast inorganic polyphophate polymerase Vtc4 crystallized by carrier-driven crystallization in fusion with the macro domain of human histone macroH2A1.1== | |
+ | <StructureSection load='5lnc' size='340' side='right' caption='[[5lnc]], [[Resolution|resolution]] 3.29Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[5lnc]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LNC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LNC FirstGlance]. <br> | ||
+ | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5iit|5iit]]</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=5lnc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lnc OCA], [http://pdbe.org/5lnc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lnc RCSB], [http://www.ebi.ac.uk/pdbsum/5lnc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lnc ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/VTC4_YEAST VTC4_YEAST]] Component of the vacuolar transporter chaperone (VTC) complex, which plays a role in vacuolar membrane fusion. Required for SEC18/NSF activity in SNARE priming, membrane binding of LMA1 and V(0) trans-complex formation.<ref>PMID:11102525</ref> <ref>PMID:11823419</ref> <ref>PMID:12584253</ref> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Obtaining well-ordered crystals remains a significant challenge in protein X-ray crystallography. Carrier-driven crystallization can facilitate crystal formation and structure solution of difficult target proteins. We obtained crystals of the small and highly flexible SPX domain from the yeast vacuolar transporter chaperone 4 (Vtc4) when fused to a C-terminal, non-cleavable macro tag derived from human histone macroH2A1.1. Initial crystals diffracted to 3.3 A resolution. Reductive protein methylation of the fusion protein yielded a new crystal form diffracting to 2.1 A. The structures were solved by molecular replacement, using isolated macro domain structures as search models. Our findings suggest that macro domain tags can be employed in recombinant protein expression in E. coli, and in carrier-driven crystallization. | ||
- | + | The macro domain as fusion tag for carrier-driven crystallization.,Wild R, Hothorn M Protein Sci. 2016 Oct 24. doi: 10.1002/pro.3073. PMID:27774698<ref>PMID:27774698</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 5lnc" style="background-color:#fffaf0;"></div> | |
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
[[Category: Hothorn, M]] | [[Category: Hothorn, M]] | ||
+ | [[Category: Wild, R]] | ||
+ | [[Category: Carrier-driven crystallization]] | ||
+ | [[Category: Hydrolase]] | ||
+ | [[Category: Inositol polyphosphate binding]] | ||
+ | [[Category: Macro domain]] | ||
+ | [[Category: Spx domain]] |
Revision as of 19:56, 9 December 2016
Structure of SPX domain of the yeast inorganic polyphophate polymerase Vtc4 crystallized by carrier-driven crystallization in fusion with the macro domain of human histone macroH2A1.1
|