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| - | [[Image:1p1c.jpg|left|200px]] | |
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| - | {{Structure
| + | ==Guanidinoacetate Methyltransferase with Gd ion== |
| - | |PDB= 1p1c |SIZE=350|CAPTION= <scene name='initialview01'>1p1c</scene>, resolution 2.5Å
| + | <StructureSection load='1p1c' size='340' side='right'caption='[[1p1c]], [[Resolution|resolution]] 2.50Å' scene=''> |
| - | |SITE=
| + | == Structural highlights == |
| - | |LIGAND= <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene> and <scene name='pdbligand=GD3:GADOLINIUM ION'>GD3</scene> | + | <table><tr><td colspan='2'>[[1p1c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P1C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P1C FirstGlance]. <br> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Guanidinoacetate_N-methyltransferase Guanidinoacetate N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.2 2.1.1.2]
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
| - | |GENE= GAMT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GD3:GADOLINIUM+ION'>GD3</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></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=1p1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p1c OCA], [https://pdbe.org/1p1c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p1c RCSB], [https://www.ebi.ac.uk/pdbsum/1p1c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p1c ProSAT]</span></td></tr> |
| - | | + | </table> |
| - | '''Guanidinoacetate Methyltransferase with Gd ion'''
| + | == Function == |
| - | | + | [https://www.uniprot.org/uniprot/GAMT_RAT GAMT_RAT] |
| - | | + | == Evolutionary Conservation == |
| - | ==Overview== | + | [[Image:Consurf_key_small.gif|200px|right]] |
| - | Guanidinoacetate methyltransferase (GAMT) is the enzyme that catalyzes the last step of creatine biosynthesis. The enzyme is found in abundance in the livers of all vertebrates. Recombinant rat liver GAMT truncated at amino acid 37 from the N-terminus has been crystallized with S-adenosylhomocysteine (SAH) in a monoclinic modification and the crystal structure has been determined at 2.8 A resolution. There are two dimers in the crystallographic asymmetric unit. Each dimer has non-crystallographic twofold symmetry and is related to the other dimer by pseudo-4(3) symmetry along the crystallographic b axis. The overall structure of GAMT crystallized in the monoclinic modification is quite similar to the structure observed in the tetragonal modification [Komoto et al. (2002), J. Mol. Biol. 320, 223-235], with the exception of the loop containing Tyr136. In the monoclinic modification, the loops in three of the four subunits have a catalytically unfavorable conformation and the loop of the fourth subunit has a catalytically favorable conformation as observed in the crystals of the tetragonal modification. From the structures in the monoclinic and tetragonal modifications, we can explain why the Y136F mutant enzyme retains considerable catalytic activity while the Y136V mutant enzyme loses the catalytic activity. The crystal structure of a Gd derivative of the tetragonal modification has also been determined. By comparing the Gd-derivative structure with the native structures in the tetragonal and the monoclinic modifications, useful characteristic features of Gd-ion binding for application in protein crystallography have been observed. Gd ions can bind to proteins without changing the native protein structures and Gd atoms produce strong anomalous dispersion signals from Cu Kalpha radiation; however, Gd-ion binding to protein requires a relatively specific geometry.
| + | Check<jmol> |
| - | | + | <jmolCheckbox> |
| - | ==About this Structure== | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p1/1p1c_consurf.spt"</scriptWhenChecked> |
| - | 1P1C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P1C OCA].
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| - | | + | <text>to colour the structure by Evolutionary Conservation</text> |
| - | ==Reference== | + | </jmolCheckbox> |
| - | Monoclinic guanidinoacetate methyltransferase and gadolinium ion-binding characteristics., Komoto J, Takata Y, Yamada T, Konishi K, Ogawa H, Gomi T, Fujioka M, Takusagawa F, Acta Crystallogr D Biol Crystallogr. 2003 Sep;59(Pt 9):1589-96. Epub 2003, Aug 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12925789 12925789]
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1p1c ConSurf]. |
| - | [[Category: Guanidinoacetate N-methyltransferase]] | + | <div style="clear:both"></div> |
| | + | __TOC__ |
| | + | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Rattus norvegicus]] | | [[Category: Rattus norvegicus]] |
| - | [[Category: Single protein]]
| + | [[Category: Komoto J]] |
| - | [[Category: Komoto, J.]] | + | [[Category: Takusagawa F]] |
| - | [[Category: Takusagawa, F.]] | + | |
| - | [[Category: GD3]]
| + | |
| - | [[Category: SAH]]
| + | |
| - | [[Category: gd ion]]
| + | |
| - | [[Category: guanidinoacetate methyltransferase]]
| + | |
| - | [[Category: methyltransferase]]
| + | |
| - | [[Category: s-adenosylhomocysteine]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:18:29 2008''
| + | |
