|
|
| (One intermediate revision not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==Crystal structure of phosphopantetheine adenylyltransferase (PPAT) in complex with ATP from Enterococcus faecalis== | | ==Crystal structure of phosphopantetheine adenylyltransferase (PPAT) in complex with ATP from Enterococcus faecalis== |
| - | <StructureSection load='3nd6' size='340' side='right' caption='[[3nd6]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='3nd6' size='340' side='right'caption='[[3nd6]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3nd6]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"enterococcus_proteiformis"_thiercelin_and_jouhaud_1903 "enterococcus proteiformis" thiercelin and jouhaud 1903]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ND6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ND6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3nd6]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ND6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ND6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</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]] 2.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3nd5|3nd5]], [[3nd7|3nd7]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">coaD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1351 "Enterococcus proteiformis" Thiercelin and Jouhaud 1903])</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=3nd6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nd6 OCA], [https://pdbe.org/3nd6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nd6 RCSB], [https://www.ebi.ac.uk/pdbsum/3nd6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nd6 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pantetheine-phosphate_adenylyltransferase Pantetheine-phosphate adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.3 2.7.7.3] </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=3nd6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nd6 OCA], [http://pdbe.org/3nd6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3nd6 RCSB], [http://www.ebi.ac.uk/pdbsum/3nd6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3nd6 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/COAD_ENTFA COAD_ENTFA]] Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate (By similarity). | + | [https://www.uniprot.org/uniprot/COAD_ENTFA COAD_ENTFA] Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 25: |
Line 23: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Enterococcus proteiformis thiercelin and jouhaud 1903]] | + | [[Category: Enterococcus faecalis]] |
| - | [[Category: Pantetheine-phosphate adenylyltransferase]] | + | [[Category: Large Structures]] |
| - | [[Category: Lee, H H]] | + | [[Category: Lee HH]] |
| - | [[Category: Suh, S W]] | + | [[Category: Suh SW]] |
| - | [[Category: Yoon, H J]] | + | [[Category: Yoon HJ]] |
| - | [[Category: Coenzyme a biosynthetic pathway]]
| + | |
| - | [[Category: Phosphopantetheine adenylyltransferase]]
| + | |
| - | [[Category: Ppat]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
COAD_ENTFA Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate (By similarity).
Publication Abstract from PubMed
Phosphopantetheine adenylyltransferase (PPAT) catalyzes the reversible transfer of an adenylyl group from ATP to 4'-phosphopantetheine (Ppant) to form dephospho-CoA (dPCoA) and pyrophosphate in the Coenzyme A (CoA) biosynthetic pathway. Importantly, PPATs are the potential target for developing antibiotics because bacterial and mammalian PPATs share little sequence homology. Previous structural studies revealed the mechanism of the recognizing substrates and products. The binding modes of ATP, ADP, Ppant, and dPCoA are highly similar in all known structures, whereas the binding modes of CoA or 3'-phosphoadenosine 5'-phosphosulfate binding are novel. To provide further structural information on ligand binding by PPATs, the crystal structure of PPAT from Enterococcus faecalis was solved in three forms: (i) apo form, (ii) binary complex with ATP, and (iii) binary complex with pantetheine. The substrate analog, pantetheine, binds to the active site in a similar manner to Ppant. The new structural information reported in this study including pantetheine as a potent inhibitor of PPAT will supplement the existing structural data and should be useful for structurebased antibacterial discovery against PPATs.
Crystal structure of phosphopantetheine adenylyltransferase from Enterococcus faecalis in the ligand-unbound state and in complex with ATP and pantetheine.,Yoon HJ, Kang JY, Mikami B, Lee HH, Suh SW Mol Cells. 2011 Nov;32(5):431-5. Epub 2011 Sep 9. PMID:21912874[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yoon HJ, Kang JY, Mikami B, Lee HH, Suh SW. Crystal structure of phosphopantetheine adenylyltransferase from Enterococcus faecalis in the ligand-unbound state and in complex with ATP and pantetheine. Mol Cells. 2011 Nov;32(5):431-5. Epub 2011 Sep 9. PMID:21912874 doi:10.1007/s10059-011-0102-y
|
