5kgl: Difference between revisions
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<StructureSection load='5kgl' size='340' side='right'caption='[[5kgl]], [[Resolution|resolution]] 2.45Å' scene=''> | <StructureSection load='5kgl' size='340' side='right'caption='[[5kgl]], [[Resolution|resolution]] 2.45Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5kgl]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KGL OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5kgl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KGL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KGL FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.45Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=5kgl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kgl OCA], [https://pdbe.org/5kgl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kgl RCSB], [https://www.ebi.ac.uk/pdbsum/5kgl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kgl ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/GPMI_CAEEL GPMI_CAEEL] Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.<ref>PMID:15234973</ref> <ref>PMID:17897734</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Caenorhabditis elegans]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Battaile | [[Category: Battaile KP]] | ||
[[Category: Carlow | [[Category: Carlow T]] | ||
[[Category: Dranchak | [[Category: Dranchak P]] | ||
[[Category: Inglese | [[Category: Inglese J]] | ||
[[Category: Li | [[Category: Li Z]] | ||
[[Category: Lovell | [[Category: Lovell S]] | ||
[[Category: MacArthur | [[Category: MacArthur R]] | ||
[[Category: Mehzabeen | [[Category: Mehzabeen N]] | ||
[[Category: Suga | [[Category: Suga H]] | ||
[[Category: Yu | [[Category: Yu H]] | ||
Latest revision as of 13:00, 27 September 2023
2.45A resolution structure of Apo independent phosphoglycerate mutase from C. elegans (orthorhombic form)2.45A resolution structure of Apo independent phosphoglycerate mutase from C. elegans (orthorhombic form)
Structural highlights
FunctionGPMI_CAEEL Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.[1] [2] Publication Abstract from PubMedGlycolytic interconversion of phosphoglycerate isomers is catalysed in numerous pathogenic microorganisms by a cofactor-independent mutase (iPGM) structurally distinct from the mammalian cofactor-dependent (dPGM) isozyme. The iPGM active site dynamically assembles through substrate-triggered movement of phosphatase and transferase domains creating a solvent inaccessible cavity. Here we identify alternate ligand binding regions using nematode iPGM to select and enrich lariat-like ligands from an mRNA-display macrocyclic peptide library containing >1012 members. Functional analysis of the ligands, named ipglycermides, demonstrates sub-nanomolar inhibition of iPGM with complete selectivity over dPGM. The crystal structure of an iPGM macrocyclic peptide complex illuminated an allosteric, locked-open inhibition mechanism placing the cyclic peptide at the bi-domain interface. This binding mode aligns the pendant lariat cysteine thiolate for coordination with the iPGM transition metal ion cluster. The extended charged, hydrophilic binding surface interaction rationalizes the persistent challenges these enzymes have presented to small-molecule screening efforts highlighting the important roles of macrocyclic peptides in expanding chemical diversity for ligand discovery. Macrocycle peptides delineate locked-open inhibition mechanism for microorganism phosphoglycerate mutases.,Yu H, Dranchak P, Li Z, MacArthur R, Munson MS, Mehzabeen N, Baird NJ, Battalie KP, Ross D, Lovell S, Carlow CK, Suga H, Inglese J Nat Commun. 2017 Apr 3;8:14932. doi: 10.1038/ncomms14932. PMID:28368002[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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