2p35: Difference between revisions
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==Crystal structure of trans-aconitate methyltransferase from Agrobacterium tumefaciens== | ==Crystal structure of trans-aconitate methyltransferase from Agrobacterium tumefaciens== | ||
<StructureSection load='2p35' size='340' side='right' caption='[[2p35]], [[Resolution|resolution]] 1.95Å' scene=''> | <StructureSection load='2p35' size='340' side='right'caption='[[2p35]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2p35]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2p35]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Agrfc Agrfc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P35 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2P35 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> | </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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tam, Atu0870, AGR_C_1589 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tam, Atu0870, AGR_C_1589 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=176299 AGRFC])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Trans-aconitate_2-methyltransferase Trans-aconitate 2-methyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.144 2.1.1.144] </span></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=2p35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p35 OCA], [https://pdbe.org/2p35 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2p35 RCSB], [https://www.ebi.ac.uk/pdbsum/2p35 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2p35 ProSAT], [https://www.topsan.org/Proteins/MCSG/2p35 TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/TAM_AGRT5 TAM_AGRT5]] Catalyzes the S-adenosylmethionine monomethyl esterification of trans-aconitate (By similarity). | ||
== 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: Agrfc]] | [[Category: Agrfc]] | ||
[[Category: Large Structures]] | |||
[[Category: Trans-aconitate 2-methyltransferase]] | [[Category: Trans-aconitate 2-methyltransferase]] | ||
[[Category: Chang, C]] | [[Category: Chang, C]] | ||
Latest revision as of 18:14, 17 June 2021
Crystal structure of trans-aconitate methyltransferase from Agrobacterium tumefaciensCrystal structure of trans-aconitate methyltransferase from Agrobacterium tumefaciens
Structural highlights
Function[TAM_AGRT5] Catalyzes the S-adenosylmethionine monomethyl esterification of trans-aconitate (By similarity). 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 PubMedWe tested the general applicability of in situ proteolysis to form protein crystals suitable for structure determination by adding a protease (chymotrypsin or trypsin) digestion step to crystallization trials of 55 bacterial and 14 human proteins that had proven recalcitrant to our best efforts at crystallization or structure determination. This is a work in progress; so far we determined structures of 9 bacterial proteins and the human aminoimidazole ribonucleotide synthetase (AIRS) domain. In situ proteolysis for protein crystallization and structure determination.,Dong A, Xu X, Edwards AM, Chang C, Chruszcz M, Cuff M, Cymborowski M, Di Leo R, Egorova O, Evdokimova E, Filippova E, Gu J, Guthrie J, Ignatchenko A, Joachimiak A, Klostermann N, Kim Y, Korniyenko Y, Minor W, Que Q, Savchenko A, Skarina T, Tan K, Yakunin A, Yee A, Yim V, Zhang R, Zheng H, Akutsu M, Arrowsmith C, Avvakumov GV, Bochkarev A, Dahlgren LG, Dhe-Paganon S, Dimov S, Dombrovski L, Finerty P Jr, Flodin S, Flores A, Graslund S, Hammerstrom M, Herman MD, Hong BS, Hui R, Johansson I, Liu Y, Nilsson M, Nedyalkova L, Nordlund P, Nyman T, Min J, Ouyang H, Park HW, Qi C, Rabeh W, Shen L, Shen Y, Sukumard D, Tempel W, Tong Y, Tresagues L, Vedadi M, Walker JR, Weigelt J, Welin M, Wu H, Xiao T, Zeng H, Zhu H Nat Methods. 2007 Dec;4(12):1019-21. Epub 2007 Nov 4. PMID:17982461[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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