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| - | [[Image:1eg2.gif|left|200px]]<br /><applet load="1eg2" size="350" color="white" frame="true" align="right" spinBox="true" | |
| - | caption="1eg2, resolution 1.75Å" /> | |
| - | '''CRYSTAL STRUCTURE OF RHODOBACTER SPHEROIDES (N6 ADENOSINE) METHYLTRANSFERASE (M.RSRI)'''<br /> | |
| | | | |
| - | ==Overview== | + | ==CRYSTAL STRUCTURE OF RHODOBACTER SPHEROIDES (N6 ADENOSINE) METHYLTRANSFERASE (M.RSRI)== |
| - | DNA methylation is important in cellular, developmental and disease processes, as well as in bacterial restriction-modification systems. Methylation of DNA at the amino groups of cytosine and adenine is a common mode of protection against restriction endonucleases afforded by the bacterial methyltransferases. The first structure of an N:6-adenine methyltransferase belonging to the beta class of bacterial methyltransferases is described here. The structure of M. RSR:I from Rhodobacter sphaeroides, which methylates the second adenine of the GAATTC sequence, was determined to 1.75 A resolution using X-ray crystallography. Like other methyltransferases, the enzyme contains the methylase fold and has well-defined substrate binding pockets. The catalytic core most closely resembles the PVU:II methyltransferase, a cytosine amino methyltransferase of the same beta group. The larger nucleotide binding pocket observed in M. RSR:I is expected because it methylates adenine. However, the most striking difference between the RSR:I methyltransferase and the other bacterial enzymes is the structure of the putative DNA target recognition domain, which is formed in part by two helices on an extended arm of the protein on the face of the enzyme opposite the active site. This observation suggests that a dramatic conformational change or oligomerization may take place during DNA binding and methylation.
| + | <StructureSection load='1eg2' size='340' side='right'caption='[[1eg2]], [[Resolution|resolution]] 1.75Å' scene=''> |
| - | | + | == Structural highlights == |
| - | ==About this Structure== | + | <table><tr><td colspan='2'>[[1eg2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cereibacter_sphaeroides Cereibacter sphaeroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EG2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EG2 FirstGlance]. <br> |
| - | 1EG2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides] with <scene name='pdbligand=MTA:'>MTA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Site-specific_DNA-methyltransferase_(adenine-specific) Site-specific DNA-methyltransferase (adenine-specific)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.72 2.1.1.72] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EG2 OCA].
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75Å</td></tr> |
| - | | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MTA:5-DEOXY-5-METHYLTHIOADENOSINE'>MTA</scene></td></tr> |
| - | ==Reference==
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1eg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eg2 OCA], [https://pdbe.org/1eg2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eg2 RCSB], [https://www.ebi.ac.uk/pdbsum/1eg2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eg2 ProSAT], [https://www.topsan.org/Proteins/MCSG/1eg2 TOPSAN]</span></td></tr> |
| - | Structure of RsrI methyltransferase, a member of the N6-adenine beta class of DNA methyltransferases., Scavetta RD, Thomas CB, Walsh MA, Szegedi S, Joachimiak A, Gumport RI, Churchill ME, Nucleic Acids Res. 2000 Oct 15;28(20):3950-61. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11024175 11024175]
| + | </table> |
| - | [[Category: Rhodobacter sphaeroides]]
| + | == Function == |
| - | [[Category: Single protein]]
| + | [https://www.uniprot.org/uniprot/MTR1_CERSP MTR1_CERSP] A beta subtype methylase, recognizes the double-stranded sequence 5'-GAATTC-3', methylates A-3 on both strands, and protects the DNA from cleavage by the RsrI endonuclease.<ref>PMID:2690017</ref> <ref>PMID:12654995</ref> |
| - | [[Category: Site-specific DNA-methyltransferase (adenine-specific)]] | + | == Evolutionary Conservation == |
| - | [[Category: Churchill, M E.A.]]
| + | [[Image:Consurf_key_small.gif|200px|right]] |
| - | [[Category: Gumport, R I.]]
| + | Check<jmol> |
| - | [[Category: Joachimiak, A.]] | + | <jmolCheckbox> |
| - | [[Category: MCSG, Midwest Center for Structural Genomics.]]
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eg/1eg2_consurf.spt"</scriptWhenChecked> |
| - | [[Category: Scavetta, R D.]]
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| - | [[Category: Szegedi, S.]] | + | <text>to colour the structure by Evolutionary Conservation</text> |
| - | [[Category: Thomas, C B.]] | + | </jmolCheckbox> |
| - | [[Category: Walsh, M A.]]
| + | </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=1eg2 ConSurf]. |
| - | [[Category: MTA]]
| + | <div style="clear:both"></div> |
| - | [[Category: dna binding]]
| + | == References == |
| - | [[Category: dna methylation]] | + | <references/> |
| - | [[Category: dna modification]] | + | __TOC__ |
| - | [[Category: exocyclic amino dna methyltransferase rsri]] | + | </StructureSection> |
| - | [[Category: mcsg]] | + | [[Category: Cereibacter sphaeroides]] |
| - | [[Category: midwest center for structural genomics]] | + | [[Category: Large Structures]] |
| - | [[Category: protein structure initiative]] | + | [[Category: Churchill MEA]] |
| - | [[Category: psi]] | + | [[Category: Gumport RI]] |
| - | [[Category: rossmann fold]] | + | [[Category: Joachimiak A]] |
| - | [[Category: structural genomics]] | + | [[Category: Scavetta RD]] |
| - | | + | [[Category: Szegedi S]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:27:22 2008''
| + | [[Category: Thomas CB]] |
| | + | [[Category: Walsh MA]] |
| Structural highlights
Function
MTR1_CERSP A beta subtype methylase, recognizes the double-stranded sequence 5'-GAATTC-3', methylates A-3 on both strands, and protects the DNA from cleavage by the RsrI endonuclease.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Kaszubska W, Aiken C, O'Connor CD, Gumport RI. Purification, cloning and sequence analysis of RsrI DNA methyltransferase: lack of homology between two enzymes, RsrI and EcoRI, that methylate the same nucleotide in identical recognition sequences. Nucleic Acids Res. 1989 Dec 25;17(24):10403-25. PMID:2690017 doi:10.1093/nar/17.24.10403
- ↑ Roberts RJ, Belfort M, Bestor T, Bhagwat AS, Bickle TA, Bitinaite J, Blumenthal RM, Degtyarev SKh, Dryden DT, Dybvig K, Firman K, Gromova ES, Gumport RI, Halford SE, Hattman S, Heitman J, Hornby DP, Janulaitis A, Jeltsch A, Josephsen J, Kiss A, Klaenhammer TR, Kobayashi I, Kong H, Kruger DH, Lacks S, Marinus MG, Miyahara M, Morgan RD, Murray NE, Nagaraja V, Piekarowicz A, Pingoud A, Raleigh E, Rao DN, Reich N, Repin VE, Selker EU, Shaw PC, Stein DC, Stoddard BL, Szybalski W, Trautner TA, Van Etten JL, Vitor JM, Wilson GG, Xu SY. A nomenclature for restriction enzymes, DNA methyltransferases, homing endonucleases and their genes. Nucleic Acids Res. 2003 Apr 1;31(7):1805-12. PMID:12654995
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