4px7

<StructureSection load='4px7' size='340' side='right' caption='[[4px7]], [[Resolution|resolution]] 3.20&Aring;' scene=''>

<table><tr><td colspan='2'>[[4px7]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PX7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PX7 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene></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=4px7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4px7 OCA], [http://pdbe.org/4px7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4px7 RCSB], [http://www.ebi.ac.uk/pdbsum/4px7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4px7 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Membrane-integrated type II phosphatidic acid phosphatases (PAP2s) are important for numerous bacterial to human biological processes, including glucose transport, lipid metabolism, and signaling. Escherichia coli phosphatidylglycerol-phosphate phosphatase B (ecPgpB) catalyzes removing the terminal phosphate group from a lipid carrier, undecaprenyl pyrophosphate, and is essential for transport of many hydrophilic small molecules across the membrane. We determined the crystal structure of ecPgpB at a resolution of 3.2 A. This structure shares a similar folding topology and a nearly identical active site with soluble PAP2 enzymes. However, the substrate binding mechanism appears to be fundamentally different from that in soluble PAP2 enzymes. In ecPgpB, the potential substrate entrance to the active site is located in a cleft formed by a V-shaped transmembrane helix pair, allowing lateral movement of the lipid substrate entering the active site from the membrane lipid bilayer. Activity assays of point mutations confirmed the importance of the catalytic residues and potential residues involved in phosphate binding. The structure also suggests an induced-fit mechanism for the substrate binding. The 3D structure of ecPgpB serves as a prototype to study eukaryotic PAP2 enzymes, including human glucose-6-phosphatase, a key enzyme in the homeostatic regulation of blood glucose concentrations.

Crystal structure of lipid phosphatase Escherichia coli phosphatidylglycerophosphate phosphatase B.,Fan J, Jiang D, Zhao Y, Liu J, Zhang XC Proc Natl Acad Sci U S A. 2014 May 12. PMID:24821770<ref>PMID:24821770</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 4px7" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Fan, J]]

[[Category: Jiang, D]]

[[Category: Zhang, X C]]

[[Category: Zhao, Y]]

[[Category: Membrane]]