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| | <StructureSection load='5dpl' size='340' side='right'caption='[[5dpl]], [[Resolution|resolution]] 3.20Å' scene=''> | | <StructureSection load='5dpl' size='340' side='right'caption='[[5dpl]], [[Resolution|resolution]] 3.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5dpl]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ricty Ricty]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DPL OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5DPL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5dpl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rickettsia_typhi_str._Wilmington Rickettsia typhi str. Wilmington]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DPL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DPL FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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]] 3.2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5dnk|5dnk]], [[5do0|5do0]], [[5doo|5doo]], [[5dpd|5dpd]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RT0101 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=257363 RICTY])</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=5dpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dpl OCA], [https://pdbe.org/5dpl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dpl RCSB], [https://www.ebi.ac.uk/pdbsum/5dpl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dpl ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5dpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dpl OCA], [http://pdbe.org/5dpl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dpl RCSB], [http://www.ebi.ac.uk/pdbsum/5dpl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dpl ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q68XQ5_RICTY Q68XQ5_RICTY] |
| | <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: Ricty]] | + | [[Category: Rickettsia typhi str. Wilmington]] |
| - | [[Category: Abeykoon, A]] | + | [[Category: Abeykoon A]] |
| - | [[Category: Buchanan, S K]] | + | [[Category: Buchanan SK]] |
| - | [[Category: He, Y]] | + | [[Category: He Y]] |
| - | [[Category: Noinaj, N]] | + | [[Category: Noinaj N]] |
| - | [[Category: Yang, D C]] | + | [[Category: Yang DC]] |
| - | [[Category: Methylation]]
| + | |
| - | [[Category: Methyltransferase]]
| + | |
| - | [[Category: Rossmann fold]]
| + | |
| - | [[Category: Sam binding protein]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
Q68XQ5_RICTY
Publication Abstract from PubMed
Rickettsia belong to a family of Gram-negative obligate-intracellular infectious bacteria that are the causative agents of typhus and spotted fever. Outer membrane protein B (OmpB) occurs in all rickettsial species, serves as a protective envelope, mediates host cell adhesion and invasion, and is a major immunodominant antigen. OmpBs from virulent strains contain multiple trimethylated lysine residues, while avirulent strain contains mainly monomethyllysine. Two protein lysine methyltransferases that catalyze methylation of recombinant OmpB at multiple sites with varying sequences have been identified and overexpressed. PKMT1 catalyzes predominantly monomethylation, while PKMT2 catalyzes mainly trimethylation. Rickettsial PKMT1 and PKMT2 are unusual in that their primary substrate appears to be limited to OmpB and both are capable of methylating multiple lysyl residues with broad sequence specificity. Here we report the crystal structures of PKMT1 from R. prowazekii and PKMT2 from R. typhi, both the apo-form and in complex with its cofactor AdoMet or AdoHcy. The structure of PKMT1 in complex with AdoHcy is solved to a resolution of 1.9 A. Both enzymes are dimeric, with each monomer containing an AdoMet binding domain with a core Rossmann fold, a dimerization domain, a middle domain, a C-terminal domain, and a centrally located open cavity. Based on the crystal structures, residues involved in catalysis, cofactor binding and substrate interactions were examined using site-directed mutagenesis followed by steady-state kinetic analysis to ascertain their catalytic functions in solution. Together, our data reveal new structural and mechanistic insights on how rickettsial methyltransferases catalyze OmpB methylation.
Structural Insights into Substrate Recognition and Catalysis in OmpB by Protein Lysine Methyltransferases from Rickettsia.,Abeykoon AH, Noinaj N, Choi BE, Wise L, He Y, Chao CC, Wang G, Gucek M, Ching WM, Chock PB, Buchanan SK, Yang DC J Biol Chem. 2016 Jul 29. pii: jbc.M116.723460. PMID:27474738[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Abeykoon AH, Noinaj N, Choi BE, Wise L, He Y, Chao CC, Wang G, Gucek M, Ching WM, Chock PB, Buchanan SK, Yang DC. Structural Insights into Substrate Recognition and Catalysis in OmpB by Protein Lysine Methyltransferases from Rickettsia. J Biol Chem. 2016 Jul 29. pii: jbc.M116.723460. PMID:27474738 doi:http://dx.doi.org/10.1074/jbc.M116.723460
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