1mlv
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1mlv]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MLV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MLV FirstGlance]. <br> | <table><tr><td colspan='2'>[[1mlv]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MLV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MLV FirstGlance]. <br> | ||
- | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> |
- | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/[Ribulose-bisphosphate_carboxylase]-lysine_N-methyltransferase [Ribulose-bisphosphate carboxylase]-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.127 2.1.1.127] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/[Ribulose-bisphosphate_carboxylase]-lysine_N-methyltransferase [Ribulose-bisphosphate carboxylase]-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.127 2.1.1.127] </span></td></tr> |
- | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mlv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mlv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1mlv RCSB], [http://www.ebi.ac.uk/pdbsum/1mlv PDBsum]</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=1mlv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mlv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1mlv RCSB], [http://www.ebi.ac.uk/pdbsum/1mlv PDBsum]</span></td></tr> |
- | <table> | + | </table> |
+ | == Function == | ||
+ | [[http://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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</StructureSection> | </StructureSection> | ||
[[Category: Pisum sativum]] | [[Category: Pisum sativum]] | ||
- | [[Category: Beach, B M | + | [[Category: Beach, B M]] |
- | [[Category: Dirk, L M.A | + | [[Category: Dirk, L M.A]] |
- | [[Category: Houtz, R L | + | [[Category: Houtz, R L]] |
- | [[Category: Hurley, J H | + | [[Category: Hurley, J H]] |
- | [[Category: Trievel, R C | + | [[Category: Trievel, R C]] |
[[Category: Lysine n-methylation]] | [[Category: Lysine n-methylation]] | ||
[[Category: Photosynthesis]] | [[Category: Photosynthesis]] |
Revision as of 08:38, 24 December 2014
Structure and Catalytic Mechanism of a SET Domain Protein Methyltransferase
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