1fjx

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[[Image:1fjx.gif|left|200px]]
 
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{{Structure
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==STRUCTURE OF TERNARY COMPLEX OF HHAI METHYLTRANSFERASE MUTANT (T250G) IN COMPLEX WITH DNA AND ADOHCY==
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|PDB= 1fjx |SIZE=350|CAPTION= <scene name='initialview01'>1fjx</scene>, resolution 2.26&Aring;
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<StructureSection load='1fjx' size='340' side='right'caption='[[1fjx]], [[Resolution|resolution]] 2.26&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>
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<table><tr><td colspan='2'>[[1fjx]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_haemolyticus Haemophilus haemolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FJX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FJX FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Deleted_entry Deleted entry], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.73 2.1.1.73]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.26&#8491;</td></tr>
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|GENE=
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<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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fjx OCA], [https://pdbe.org/1fjx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fjx RCSB], [https://www.ebi.ac.uk/pdbsum/1fjx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fjx ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MTH1_HAEPH MTH1_HAEPH] This methylase recognizes the double-stranded sequence GCGC, causes specific methylation on C-2 on both strands, and protects the DNA from cleavage by the HhaI endonuclease.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fj/1fjx_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1fjx ConSurf].
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<div style="clear:both"></div>
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'''STRUCTURE OF TERNARY COMPLEX OF HHAI METHYLTRANSFERASE MUTANT (T250G) IN COMPLEX WITH DNA AND ADOHCY'''
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==See Also==
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*[[DNA methyltransferase 3D structures|DNA methyltransferase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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DNA cytosine-5-methyltransferase HhaI recognizes the GCGC sequence and flips the inner cytosine out of DNA helix and into the catalytic site for methylation. The 5'-phosphate of the flipped out cytosine is in contact with the conserved Thr-250 from the target recognition domain. We have produced 12 mutants of Thr-250 and examined their methylation potential in vivo. Six active mutants were subjected to detailed biochemical and structural studies. Mutants with similar or smaller side chains (Ser, Cys, and Gly) are very similar to wild-type enzyme in terms of steady-state kinetic parameters k(cat), K(m)(DNA), K(m)(AdoMet). In contrast, the mutants with bulkier side chains (Asn, Asp, and His) show increased K(m) values for both substrates. Fluorescence titrations and stopped-flow kinetic analysis of interactions with duplex oligonucleotides containing 2-aminopurine at the target base position indicate that the T250G mutation leads to a more polar but less solvent-accessible position of the flipped out target base. The x-ray structure of the ternary M. HhaI(T250G).DNA.AdoHcy complex shows that the target cytosine is locked in the catalytic center of enzyme. The space created by the mutation is filled by water molecules and the adjacent DNA backbone atoms dislocate slightly toward the missing side chain. In aggregate, our results suggest that the side chain of Thr-250 is involved in constraining the conformation the DNA backbone and the target base during its rotation into the catalytic site of enzyme.
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==About this Structure==
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1FJX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_haemolyticus Haemophilus haemolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FJX OCA].
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==Reference==
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Functional roles of the conserved threonine 250 in the target recognition domain of HhaI DNA methyltransferase., Vilkaitis G, Dong A, Weinhold E, Cheng X, Klimasauskas S, J Biol Chem. 2000 Dec 8;275(49):38722-30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11102456 11102456]
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[[Category: Deleted entry]]
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[[Category: Haemophilus haemolyticus]]
[[Category: Haemophilus haemolyticus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Cheng, X.]]
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[[Category: Cheng X]]
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[[Category: Dong, A.]]
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[[Category: Dong A]]
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[[Category: Klimasauskas, S.]]
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[[Category: Klimasauskas S]]
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[[Category: Vilkaitis, G.]]
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[[Category: Vilkaitis G]]
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[[Category: Weinhold, E.]]
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[[Category: Weinhold E]]
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[[Category: SAH]]
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[[Category: SO4]]
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[[Category: adomet-dependent methyltransferase fold protein-dna-cofactor complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:10:07 2008''
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Current revision

STRUCTURE OF TERNARY COMPLEX OF HHAI METHYLTRANSFERASE MUTANT (T250G) IN COMPLEX WITH DNA AND ADOHCY

PDB ID 1fjx

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