We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1fjx

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1fjx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fjx, resolution 2.26&Aring;" /> '''STRUCTURE OF TERNARY...)
Current revision (07:15, 7 February 2024) (edit) (undo)
 
(17 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1fjx.gif|left|200px]]<br /><applet load="1fjx" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1fjx, resolution 2.26&Aring;" />
 
-
'''STRUCTURE OF TERNARY COMPLEX OF HHAI METHYLTRANSFERASE MUTANT (T250G) IN COMPLEX WITH DNA AND ADOHCY'''<br />
 
-
==Overview==
+
==STRUCTURE OF TERNARY COMPLEX OF HHAI METHYLTRANSFERASE MUTANT (T250G) IN COMPLEX WITH DNA AND ADOHCY==
-
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.
+
<StructureSection load='1fjx' size='340' side='right'caption='[[1fjx]], [[Resolution|resolution]] 2.26&Aring;' scene=''>
 +
== Structural highlights ==
 +
<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>
 +
</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>
 +
<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>
 +
<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>
 +
</table>
 +
== Function ==
 +
[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.
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fj/1fjx_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</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].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
1FJX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_haemolyticus Haemophilus haemolyticus] with SO4 and SAH as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FJX OCA].
+
*[[DNA methyltransferase 3D structures|DNA methyltransferase 3D structures]]
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=11102456 11102456]
+
-
[[Category: Deleted entry]]
+
[[Category: Haemophilus haemolyticus]]
[[Category: Haemophilus haemolyticus]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Cheng, X.]]
+
[[Category: Cheng X]]
-
[[Category: Dong, A.]]
+
[[Category: Dong A]]
-
[[Category: Klimasauskas, S.]]
+
[[Category: Klimasauskas S]]
-
[[Category: Vilkaitis, G.]]
+
[[Category: Vilkaitis G]]
-
[[Category: Weinhold, E.]]
+
[[Category: Weinhold E]]
-
[[Category: SAH]]
+
-
[[Category: SO4]]
+
-
[[Category: adomet-dependent methyltransferase fold protein-dna-cofactor complex]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:59:31 2007''
+

Current revision

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

PDB ID 1fjx

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1fjx"
Personal tools