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2p35

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Revision as of 14:31, 24 December 2014

Crystal structure of trans-aconitate methyltransferase from Agrobacterium tumefaciens

Structural highlights

2p35 is a 2 chain structure with sequence from Agrobacterium tumefaciens str. c58. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Gene:	tam, Atu0870, AGR_C_1589 (Agrobacterium tumefaciens str. C58)
Activity:	Trans-aconitate 2-methyltransferase, with EC number 2.1.1.144
Resources:	FirstGlance, OCA, RCSB, PDBsum, TOPSAN

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 PubMed

We 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

↑ 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. In situ proteolysis for protein crystallization and structure determination. Nat Methods. 2007 Dec;4(12):1019-21. Epub 2007 Nov 4. PMID:17982461 doi:http://dx.doi.org/10.1038/nmeth1118

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2p35"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2p35]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Agrobacterium_tumefaciens_str._c58 Agrobacterium tumefaciens str. c58]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2P35 FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene><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>
-<tr><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><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tam, Atu0870, AGR_C_1589 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=176299 Agrobacterium tumefaciens str. C58])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tam, Atu0870, AGR_C_1589 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=176299 Agrobacterium tumefaciens str. C58])</td></tr>
-<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trans-aconitate_2-methyltransferase Trans-aconitate 2-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.144 2.1.1.144] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trans-aconitate_2-methyltransferase Trans-aconitate 2-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.144 2.1.1.144] </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=2p35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p35 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2p35 RCSB], [http://www.ebi.ac.uk/pdbsum/2p35 PDBsum], [http://www.topsan.org/Proteins/MCSG/2p35 TOPSAN]</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=2p35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p35 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2p35 RCSB], [http://www.ebi.ac.uk/pdbsum/2p35 PDBsum], [http://www.topsan.org/Proteins/MCSG/2p35 TOPSAN]</span></td></tr>
-<table>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/TAM_AGRT5 TAM_AGRT5]] Catalyzes the S-adenosylmethionine monomethyl esterification of trans-aconitate (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 33: / Line 35: @@
 [[Category: Agrobacterium tumefaciens str. c58]]
 [[Category: Trans-aconitate 2-methyltransferase]]
-[[Category: Chang, C.]]
+[[Category: Chang, C]]
-[[Category: Edwards, A M.]]
+[[Category: Edwards, A M]]
-[[Category: Joachimiak, A.]]
+[[Category: Joachimiak, A]]
-[[Category: MCSG, Midwest Center for Structural Genomics.]]
+[[Category: Structural genomic]]
-[[Category: Savchenko, A.]]
+[[Category: Savchenko, A]]
-[[Category: Xu, X.]]
+[[Category: Xu, X]]
-[[Category: Zheng, H.]]
+[[Category: Zheng, H]]
 [[Category: Agrobacterium tumefacien]]
 [[Category: Mcsg]]
-[[Category: Midwest center for structural genomic]]
+[[Category: PSI, Protein structure initiative]]
-[[Category: Protein structure initiative]]
-[[Category: Psi-2]]
 [[Category: Sam dependent methyltransferase]]
-[[Category: Structural genomic]]
 [[Category: Trans-aconitate methyltransferase]]
 [[Category: Transferase]]

2p35

From Proteopedia

Revision as of 14:31, 24 December 2014

Crystal structure of trans-aconitate methyltransferase from Agrobacterium tumefaciens

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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