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| | <StructureSection load='1ozv' size='340' side='right'caption='[[1ozv]], [[Resolution|resolution]] 2.65Å' scene=''> | | <StructureSection load='1ozv' size='340' side='right'caption='[[1ozv]], [[Resolution|resolution]] 2.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1ozv]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Garden_pea Garden pea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OZV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OZV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1ozv]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OZV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OZV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LYS:LYSINE'>LYS</scene>, <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]] 2.65Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1mlv|1mlv]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LYS:LYSINE'>LYS</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/[Ribulose-bisphosphate_carboxylase]-lysine_N-methyltransferase [Ribulose-bisphosphate carboxylase]-lysine N-methyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.127 2.1.1.127] </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=1ozv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ozv OCA], [https://pdbe.org/1ozv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ozv RCSB], [https://www.ebi.ac.uk/pdbsum/1ozv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ozv ProSAT]</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=1ozv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ozv OCA], [https://pdbe.org/1ozv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ozv RCSB], [https://www.ebi.ac.uk/pdbsum/1ozv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ozv ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/RBCMT_PEA RBCMT_PEA]] Methylates 'Lys-14' of the large subunit of RuBisCO. Can also use with lower efficiency chloroplastic fructose-bisphosphate aldolases and gamma-tocopherol methyltransferase as substrates, but not a cytosolic aldolase.<ref>PMID:22547063</ref>
| + | [https://www.uniprot.org/uniprot/RBCMT_PEA RBCMT_PEA] Methylates 'Lys-14' of the large subunit of RuBisCO. Can also use with lower efficiency chloroplastic fructose-bisphosphate aldolases and gamma-tocopherol methyltransferase as substrates, but not a cytosolic aldolase.<ref>PMID:22547063</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Garden pea]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Flynn, E M]] | + | [[Category: Pisum sativum]] |
| - | [[Category: Houtz, R L]] | + | [[Category: Flynn EM]] |
| - | [[Category: Hurley, J H]] | + | [[Category: Houtz RL]] |
| - | [[Category: Trievel, R C]] | + | [[Category: Hurley JH]] |
| - | [[Category: Lysine n-methylation]] | + | [[Category: Trievel RC]] |
| - | [[Category: Multiple methylation]]
| + | |
| - | [[Category: Photosynthesis]]
| + | |
| - | [[Category: Post-translational modification]]
| + | |
| - | [[Category: Set domain]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
RBCMT_PEA Methylates 'Lys-14' of the large subunit of RuBisCO. Can also use with lower efficiency chloroplastic fructose-bisphosphate aldolases and gamma-tocopherol methyltransferase as substrates, but not a cytosolic aldolase.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
SET domain protein methyltransferases catalyze the transfer of methyl groups from the cofactor S-adenosylmethionine (AdoMet) to specific lysine residues of protein substrates, such as the N-terminal tails of histones H3 and H4 and the large subunit of the Rubisco holoenzyme complex. The crystal structures of pea Rubisco large subunit methyltransferase (LSMT) in ternary complexes with either lysine or epsilon-N-methyllysine (MeLys) and the product S-adenosylhomocysteine (AdoHcy) were determined to resolutions of 2.65 and 2.55 A, respectively. The zeta-methyl group of MeLys is bound to the enzyme via carbon-oxygen hydrogen bonds that play a key role in catalysis. The methyl donor and acceptor are aligned in a linear geometry for S(N)2 nucleophilic transfer of the methyl group during catalysis. Differences in hydrogen bonding between the MeLys epsilon-amino group and Rubisco LSMT and SET7/9 explain why Rubisco LSMT generates multiply methylated Lys, wheras SET7/9 generates only MeLys.
Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT.,Trievel RC, Flynn EM, Houtz RL, Hurley JH Nat Struct Biol. 2003 Jul;10(7):545-52. PMID:12819771[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Mininno M, Brugiere S, Pautre V, Gilgen A, Ma S, Ferro M, Tardif M, Alban C, Ravanel S. Characterization of chloroplastic fructose 1,6-bisphosphate aldolases as lysine-methylated proteins in plants. J Biol Chem. 2012 Jun 15;287(25):21034-44. doi: 10.1074/jbc.M112.359976. Epub, 2012 Apr 30. PMID:22547063 doi:http://dx.doi.org/10.1074/jbc.M112.359976
- ↑ Trievel RC, Flynn EM, Houtz RL, Hurley JH. Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT. Nat Struct Biol. 2003 Jul;10(7):545-52. PMID:12819771 doi:http://dx.doi.org/10.1038/nsb946
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