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4o6n

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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4o6n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o6n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o6n RCSB], [http://www.ebi.ac.uk/pdbsum/4o6n PDBsum]</span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4o6n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o6n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o6n RCSB], [http://www.ebi.ac.uk/pdbsum/4o6n PDBsum]</span></td></tr>
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== Publication Abstract from PubMed ==
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The CDP-alcohol phosphotransferase (CDP-AP) family of integral membrane enzymes catalyses the transfer of a substituted phosphate group from a CDP-linked donor to an alcohol acceptor. This is an essential reaction for phospholipid biosynthesis across all kingdoms of life, and it is catalysed solely by CDP-APs. Here we report the 2.0 A resolution crystal structure of a representative CDP-AP from Archaeoglobus fulgidus. The enzyme (AF2299) is a homodimer, with each protomer consisting of six transmembrane helices and an N-terminal cytosolic domain. A polar cavity within the membrane accommodates the active site, lined with the residues from an absolutely conserved CDP-AP signature motif (D(1)xxD(2)G(1)xxAR...G(2)xxxD(3)xxxD(4)). Structures in the apo, CMP-bound, CDP-bound and CDP-glycerol-bound states define functional roles for each of these eight conserved residues and allow us to propose a sequential, base-catalysed mechanism universal for CDP-APs, in which the fourth aspartate (D4) acts as the catalytic base.
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Structural basis for catalysis in a CDP-alcohol phosphotransferase.,Sciara G, Clarke OB, Tomasek D, Kloss B, Tabuso S, Byfield R, Cohn R, Banerjee S, Rajashankar KR, Slavkovic V, Graziano JH, Shapiro L, Mancia F Nat Commun. 2014 Jun 13;5:4068. doi: 10.1038/ncomms5068. PMID:24923293<ref>PMID:24923293</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
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<references/>
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</StructureSection>
</StructureSection>

Revision as of 06:21, 13 August 2014

Structure of AF2299, a CDP-alcohol phosphotransferase (CDP-bound)

4o6n, resolution 2.10Å

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