|
|
| Line 1: |
Line 1: |
| | | | |
| | ==IMISX-EP of W-PgpB== | | ==IMISX-EP of W-PgpB== |
| - | <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 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> | + | <table><tr><td colspan='2'>[[6fmx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. 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 [https://proteopedia.org/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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.79Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='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'>[https://proteopedia.org/fgij/fg.htm?mol=6fmx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fmx OCA], [https://pdbe.org/6fmx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6fmx RCSB], [https://www.ebi.ac.uk/pdbsum/6fmx PDBsum], [https://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> | + | |
| | </table> | | </table> |
| | == 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> | + | [https://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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 24: |
Line 23: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacsu]] | + | [[Category: Bacillus subtilis subsp. subtilis str. 168]] |
| - | [[Category: Phosphatidylglycerophosphatase]] | + | [[Category: Large Structures]] |
| - | [[Category: Basu, S]] | + | [[Category: Basu S]] |
| - | [[Category: Caffrey, M]] | + | [[Category: Caffrey M]] |
| - | [[Category: Diederichs, K]] | + | [[Category: Diederichs K]] |
| - | [[Category: Howe, N]] | + | [[Category: Howe N]] |
| - | [[Category: Huang, C Y]] | + | [[Category: Huang C-Y]] |
| - | [[Category: Olieric, V]] | + | [[Category: Olieric V]] |
| - | [[Category: Panepucci, E]] | + | [[Category: Panepucci E]] |
| - | [[Category: Vogeley, L]] | + | [[Category: Vogeley L]] |
| - | [[Category: Wang, M]] | + | [[Category: Wang M]] |
| - | [[Category: Warshamanage, R]] | + | [[Category: Warshamanage R]] |
| - | [[Category: Weinert, T]] | + | [[Category: Weinert T]] |
| - | [[Category: Experimental phasing]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: In meso crystallization]]
| + | |
| - | [[Category: In situ diffraction data collection]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Membrane protein structure]]
| + | |
| - | [[Category: Serial crystallography]]
| + | |
| 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 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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ghachi ME, Howe N, Auger R, Lambion A, Guiseppi A, Delbrassine F, Manat G, Roure S, Peslier S, Sauvage E, Vogeley L, Rengifo-Gonzalez JC, Charlier P, Mengin-Lecreulx D, Foglino M, Touze T, Caffrey M, Kerff F. Crystal structure and biochemical characterization of the transmembrane PAP2 type phosphatidylglycerol phosphate phosphatase from Bacillus subtilis. Cell Mol Life Sci. 2017 Feb 6. doi: 10.1007/s00018-017-2464-6. PMID:28168443 doi:http://dx.doi.org/10.1007/s00018-017-2464-6
- ↑ Huang CY, Olieric V, Howe N, Warshamanage R, Weinert T, Panepucci E, Vogeley L, Basu S, Diederichs K, Caffrey M, Wang M. In situ serial crystallography for rapid de novo membrane protein structure determination. Commun Biol. 2018 Aug 27;1:124. doi: 10.1038/s42003-018-0123-6. eCollection 2018. PMID:30272004 doi:http://dx.doi.org/10.1038/s42003-018-0123-6
|
