1y9i
From Proteopedia
(Difference between revisions)
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==Crystal structure of low temperature requirement C protein from Listeria monocytogenes== | ==Crystal structure of low temperature requirement C protein from Listeria monocytogenes== | ||
| - | <StructureSection load='1y9i' size='340' side='right'caption='[[1y9i]]' scene=''> | + | <StructureSection load='1y9i' size='340' side='right'caption='[[1y9i]], [[Resolution|resolution]] 1.80Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y9I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y9I FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1y9i]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y9I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y9I FirstGlance]. <br> |
| - | </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=1y9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y9i OCA], [https://pdbe.org/1y9i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y9i RCSB], [https://www.ebi.ac.uk/pdbsum/1y9i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y9i ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/1y9i TOPSAN]</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]] 1.8Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1y9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y9i OCA], [https://pdbe.org/1y9i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y9i RCSB], [https://www.ebi.ac.uk/pdbsum/1y9i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y9i ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/1y9i TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q8Y4N7_LISMO Q8Y4N7_LISMO] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1y9i ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1y9i ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Phosphatidylglycerophosphatase (PGPase), an enzyme involved in lipid metabolism, catalyzes formation of phosphatidylglycerol from phosphatidylglycerophosphate. Phosphatidylglycerol is a multifunctional phospholipid, found in the biological membranes of many organisms. Here, we report the crystal structure of Listeria monocytogenes PGPase at 1.8 A resolution. PGPase, an all-helical molecule, forms a homotetramer. Each protomer contains an independent active site with two metal ions, Ca(2+) and Mg(2+), forming a hetero-binuclear center located in a hydrophilic cavity near the surface of the molecule. The binuclear center, conserved ligands, metal-bound water molecules, and an Asp-His dyad form the active site. The catalytic mechanism of this enzyme is likely to proceed via binuclear metal activated nucleophilic water. The binuclear metal-binding active-site environment of this structure should provide insights into substrate binding and metal-dependent catalysis. A long channel with inter-linked linear water chains, termed "proton wires," is observed at the tetramer interface. Comparison of similar water chain structures in photosynthetic reaction centers (RCs), Cytochrome f, gramicidin, and bacteriorhodopsin, suggests that PGPase may conduct protons via proton wires. | ||
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| + | Crystal structure of phosphatidylglycerophosphatase (PGPase), a putative membrane-bound lipid phosphatase, reveals a novel binuclear metal binding site and two "proton wires".,Kumaran D, Bonanno JB, Burley SK, Swaminathan S Proteins. 2006 Sep 1;64(4):851-62. PMID:16838328<ref>PMID:16838328</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 1y9i" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Listeria monocytogenes]] | ||
[[Category: Burley SK]] | [[Category: Burley SK]] | ||
[[Category: Kumaran D]] | [[Category: Kumaran D]] | ||
[[Category: Swaminathan S]] | [[Category: Swaminathan S]] | ||
Revision as of 08:01, 15 May 2024
Crystal structure of low temperature requirement C protein from Listeria monocytogenes
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