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==Structure of AF2299, a CDP-alcohol phosphotransferase (CMP-bound)==
==Structure of AF2299, a CDP-alcohol phosphotransferase (CMP-bound)==
<StructureSection load='4o6m' size='340' side='right' caption='[[4o6m]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='4o6m' size='340' side='right'caption='[[4o6m]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4o6m]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O6M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O6M FirstGlance]. <br>
<table><tr><td colspan='2'>[[4o6m]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus_DSM_4304 Archaeoglobus fulgidus DSM 4304]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O6M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O6M FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=C5P:CYTIDINE-5-MONOPHOSPHATE'>C5P</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MPG:1-MONOOLEOYL-RAC-GLYCEROL'>MPG</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]] 1.901&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4o6n|4o6n]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C5P:CYTIDINE-5-MONOPHOSPHATE'>C5P</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MPG:[(Z)-OCTADEC-9-ENYL]+(2R)-2,3-BIS(OXIDANYL)PROPANOATE'>MPG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4o6m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o6m OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o6m RCSB], [http://www.ebi.ac.uk/pdbsum/4o6m PDBsum]</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=4o6m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o6m OCA], [https://pdbe.org/4o6m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o6m RCSB], [https://www.ebi.ac.uk/pdbsum/4o6m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o6m ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/O27985_ARCFU O27985_ARCFU]
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.
 
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>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
==See Also==
</div>
*[[Phosphotransferase 3D structures|Phosphotransferase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Banerjee, S]]
[[Category: Archaeoglobus fulgidus DSM 4304]]
[[Category: Clarke, O B]]
[[Category: Large Structures]]
[[Category: Mancia, F]]
[[Category: Banerjee S]]
[[Category: NYCOMPS, New York Consortium on Membrane Protein Structure]]
[[Category: Clarke OB]]
[[Category: Rajashankar, K R]]
[[Category: Mancia F]]
[[Category: Sciara, G]]
[[Category: Rajashankar KR]]
[[Category: Shapiro, L]]
[[Category: Sciara G]]
[[Category: Tomasek, D]]
[[Category: Shapiro L]]
[[Category: Cdp-alcohol phosphotransferase]]
[[Category: Tomasek D]]
[[Category: Membrane protein]]
[[Category: New york consortium on membrane protein structure]]
[[Category: Nycomp]]
[[Category: Psi-biology]]
[[Category: Structural genomic]]
[[Category: Transferase]]
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