5o06: Difference between revisions
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<StructureSection load='5o06' size='340' side='right'caption='[[5o06]], [[Resolution|resolution]] 1.55Å' scene=''> | <StructureSection load='5o06' size='340' side='right'caption='[[5o06]], [[Resolution|resolution]] 1.55Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5o06]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5O06 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5o06]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacteroides_abscessus_ATCC_19977 Mycobacteroides abscessus ATCC 19977]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5O06 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5O06 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.547Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5o06 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o06 OCA], [https://pdbe.org/5o06 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5o06 RCSB], [https://www.ebi.ac.uk/pdbsum/5o06 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5o06 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/COAD_MYCA9 COAD_MYCA9] Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mycobacteroides abscessus ATCC 19977]] | ||
[[Category: Blaszczyk | [[Category: Blaszczyk M]] | ||
[[Category: Blundell | [[Category: Blundell TL]] | ||
[[Category: Kim | [[Category: Kim SY]] | ||
[[Category: Mendes | [[Category: Mendes V]] | ||
[[Category: Thomas | [[Category: Thomas SE]] | ||
Latest revision as of 15:18, 22 November 2023
Crystal structure of APO form of Phosphopantetheine adenylyltransferase from Mycobacterium abcessusCrystal structure of APO form of Phosphopantetheine adenylyltransferase from Mycobacterium abcessus
Structural highlights
FunctionCOAD_MYCA9 Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. Publication Abstract from PubMedInterest in applications of protein crystallography to medicine was evident, as the first high-resolution structures emerged in the 50s and 60s. In Cambridge, Max Perutz and John Kendrew sought to understand mutations in sickle cell and other genetic diseases related to hemoglobin, while in Oxford, the group of Dorothy Hodgkin became interested in long-lasting zinc-insulin crystals for treatment of diabetes and later considered insulin redesign, as synthetic insulins became possible. The use of protein crystallography in structure-guided drug discovery emerged as enzyme structures allowed the identification of potential inhibitor-binding sites and optimization of interactions of hits using the structure of the target protein. Early examples of this approach were the use of the structure of renin to design antihypertensives and the structure of HIV protease in design of AIDS antivirals. More recently, use of structure-guided design with fragment-based drug discovery, which reduces the size of screening libraries by decreasing complexity, has improved ligand efficiency in drug design and has been used to progress three oncology drugs through clinical trials to FDA approval. We exemplify current developments in structure-guided target identification and fragment-based lead discovery with efforts to develop new antimicrobials for mycobacterial infections. Structural Biology and the Design of New Therapeutics: From HIV and Cancer to Mycobacterial Infections: A Paper Dedicated to John Kendrew.,Thomas SE, Mendes V, Kim SY, Malhotra S, Ochoa-Montano B, Blaszczyk M, Blundell TL J Mol Biol. 2017 Aug 18;429(17):2677-2693. doi: 10.1016/j.jmb.2017.06.014. Epub, 2017 Jun 23. PMID:28648615[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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