6fmx: Difference between revisions
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<StructureSection load='6fmx' size='340' side='right' caption='[[6fmx]], [[Resolution|resolution]] 1.79Å' scene=''> | <StructureSection load='6fmx' size='340' side='right' caption='[[6fmx]], [[Resolution|resolution]] 1.79Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6fmx]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FMX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FMX FirstGlance]. <br> | <table><tr><td colspan='2'>[[6fmx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FMX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FMX FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=WO4:TUNGSTATE(VI)ION'>WO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=WO4:TUNGSTATE(VI)ION'>WO4</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pgpB, yodM, BSU19650 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphatidylglycerophosphatase Phosphatidylglycerophosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.27 3.1.3.27] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphatidylglycerophosphatase Phosphatidylglycerophosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.27 3.1.3.27] </span></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=6fmx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fmx OCA], [http://pdbe.org/6fmx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fmx RCSB], [http://www.ebi.ac.uk/pdbsum/6fmx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fmx ProSAT]</span></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=6fmx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fmx OCA], [http://pdbe.org/6fmx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fmx RCSB], [http://www.ebi.ac.uk/pdbsum/6fmx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fmx ProSAT]</span></td></tr> | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/PGPB_BACSU PGPB_BACSU]] Catalyzes the dephosphorylation of phosphatidylglycerophosphate (PGP) to phosphatidylglycerol. Also has undecaprenyl pyrophosphate phosphatase activity, required for the biosynthesis of the lipid carrier undecaprenyl phosphate.<ref>PMID:28168443</ref> | [[http://www.uniprot.org/uniprot/PGPB_BACSU PGPB_BACSU]] Catalyzes the dephosphorylation of phosphatidylglycerophosphate (PGP) to phosphatidylglycerol. Also has undecaprenyl pyrophosphate phosphatase activity, required for the biosynthesis of the lipid carrier undecaprenyl phosphate.<ref>PMID:28168443</ref> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
De novo membrane protein structure determination is often limited by the availability of large crystals and the difficulties in obtaining accurate diffraction data for experimental phasing. Here we present a method that combines in situ serial crystallography with de novo phasing for fast, efficient membrane protein structure determination. The method enables systematic diffraction screening and rapid data collection from hundreds of microcrystals in in meso crystallization wells without the need for direct crystal harvesting. The requisite data quality for experimental phasing is achieved by accumulating diffraction signals from isomorphous crystals identified post-data collection. The method works in all experimental phasing scenarios and is particularly attractive with fragile, weakly diffracting microcrystals. The automated serial data collection approach can be readily adopted at most microfocus macromolecular crystallography beamlines. | |||
In situ serial crystallography for rapid de novo membrane protein structure determination.,Huang CY, Olieric V, Howe N, Warshamanage R, Weinert T, Panepucci E, Vogeley L, Basu S, Diederichs K, Caffrey M, Wang M Commun Biol. 2018 Aug 27;1:124. doi: 10.1038/s42003-018-0123-6. eCollection 2018. PMID:30272004<ref>PMID:30272004</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6fmx" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bacsu]] | |||
[[Category: Phosphatidylglycerophosphatase]] | [[Category: Phosphatidylglycerophosphatase]] | ||
[[Category: Basu, S]] | [[Category: Basu, S]] | ||
Revision as of 11:37, 10 October 2018
IMISX-EP of W-PgpBIMISX-EP of W-PgpB
Structural highlights
Function[PGPB_BACSU] Catalyzes the dephosphorylation of phosphatidylglycerophosphate (PGP) to phosphatidylglycerol. Also has undecaprenyl pyrophosphate phosphatase activity, required for the biosynthesis of the lipid carrier undecaprenyl phosphate.[1] Publication Abstract from PubMedDe novo membrane protein structure determination is often limited by the availability of large crystals and the difficulties in obtaining accurate diffraction data for experimental phasing. Here we present a method that combines in situ serial crystallography with de novo phasing for fast, efficient membrane protein structure determination. The method enables systematic diffraction screening and rapid data collection from hundreds of microcrystals in in meso crystallization wells without the need for direct crystal harvesting. The requisite data quality for experimental phasing is achieved by accumulating diffraction signals from isomorphous crystals identified post-data collection. The method works in all experimental phasing scenarios and is particularly attractive with fragile, weakly diffracting microcrystals. The automated serial data collection approach can be readily adopted at most microfocus macromolecular crystallography beamlines. In situ serial crystallography for rapid de novo membrane protein structure determination.,Huang CY, Olieric V, Howe N, Warshamanage R, Weinert T, Panepucci E, Vogeley L, Basu S, Diederichs K, Caffrey M, Wang M Commun Biol. 2018 Aug 27;1:124. doi: 10.1038/s42003-018-0123-6. eCollection 2018. PMID:30272004[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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