6cb2: Difference between revisions

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 ==Crystal structure of Escherichia coli UppP==
-<StructureSection load='6cb2' size='340' side='right' caption='[[6cb2]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='6cb2' size='340' side='right'caption='[[6cb2]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6cb2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Eco57 Eco57]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CB2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CB2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6cb2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CB2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CB2 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=SO4:SULFATE+ION'>SO4</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]] 2&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">uppP, bacA, upk, b3057, JW3029 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57])</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=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Undecaprenyl-diphosphate_phosphatase Undecaprenyl-diphosphate phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.27 3.6.1.27] </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=6cb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cb2 OCA], [https://pdbe.org/6cb2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cb2 RCSB], [https://www.ebi.ac.uk/pdbsum/6cb2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cb2 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=6cb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cb2 OCA], [http://pdbe.org/6cb2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cb2 RCSB], [http://www.ebi.ac.uk/pdbsum/6cb2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cb2 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/UPPP_ECOLI UPPP_ECOLI]] Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.<ref>PMID:15778224</ref>
+[https://www.uniprot.org/uniprot/UPPP_ECO57 UPPP_ECO57] Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Undecaprenyl pyrophosphate phosphatase (UppP) is an integral membrane protein that recycles the lipid carrier essential to the ongoing biosynthesis of the bacterial cell wall. Individual building blocks of peptidoglycan are assembled in the cytoplasm on undecaprenyl phosphate (C55-P) before being flipped to the periplasmic face, where they are polymerized and transferred to the existing cell wall sacculus, resulting in the side product undecaprenyl pyrophosphate (C55-PP). Interruption of UppP's regeneration of C55-P from C55-PP leads to the buildup of cell wall intermediates and cell lysis. We present the crystal structure of UppP from Escherichia coli at 2.0 A resolution, which reveals the mechanistic basis for intramembranal phosphatase action and substrate specificity using an inverted topology repeat. In addition, the observation of key structural motifs common to a variety of cross membrane transporters hints at a potential flippase function in the specific relocalization of the C55-P product back to the cytosolic space.
-Crystal structure of an intramembranal phosphatase central to bacterial cell-wall peptidoglycan biosynthesis and lipid recycling.,Workman SD, Worrall LJ, Strynadka NCJ Nat Commun. 2018 Mar 20;9(1):1159. doi: 10.1038/s41467-018-03547-8. PMID:29559664<ref>PMID:29559664</ref>
+==See Also==
+*[[Undecaprenyl pyrophosphate synthase 3D structures|Undecaprenyl pyrophosphate synthase 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 6cb2" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Eco57]]
+[[Category: Escherichia coli K-12]]
-[[Category: Undecaprenyl-diphosphate phosphatase]]
+[[Category: Large Structures]]
-[[Category: Strynadka, N C.J]]
+[[Category: Strynadka NCJ]]
-[[Category: Workman, S D]]
+[[Category: Workman SD]]
-[[Category: Worrall, L J]]
+[[Category: Worrall LJ]]
-[[Category: Hydrolase]]
-[[Category: Phosphatase]]
-[[Category: Pyrophosphate]]
-[[Category: Undecaprenyl]]