2g1p

From Proteopedia

(Difference between revisions)

Revision as of 06:55, 20 June 2018

Structure of E. coli DNA adenine methyltransferase (DAM)

Structural highlights

2g1p is a 4 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1fy3, 1yfj, 1yfl, 1q0t, 1q0s
Gene:	dam ("Bacillus coli" Migula 1895)
Activity:	Site-specific DNA-methyltransferase (adenine-specific), with EC number 2.1.1.72
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[DMA_ECOLI] Methylates DNA within the sequence GATC and protects the DNA from cleavage by the restriction endonuclease MboI. Although it shares sequence specificity with a number of type II restriction endonucleases and methylases, it is thought to act in postreplication mismatch repair rather than as a part of a restriction modification system. May also play a role in DNA replication.

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

The structure of the Escherichia coli Dam DNA-(adenine-N6)-methyltransferase in complex with cognate DNA was determined at 1.89 A resolution in the presence of S-adenosyl-L-homocysteine. DNA recognition and the dynamics of base-flipping were studied by site-directed mutagenesis, DNA methylation kinetics and fluorescence stopped-flow experiments. Our data illustrate the mechanism of coupling of DNA recognition and base-flipping. Contacts to the non-target strand in the second (3') half of the GATC site are established by R124 to the fourth base-pair, and by L122 and P134 to the third base-pair. The aromatic ring of Y119 intercalates into the DNA between the second and third base-pairs, which is essential for base-flipping to occur. Compared to previous published structures of bacteriophage T4 Dam, three major new observations are made in E.coli Dam. (1) The first Gua is recognized by K9, removal of which abrogates the first base-pair recognition. (2) The flipped target Ade binds to the surface of EcoDam in the absence of S-adenosyl-L-methionine, which illustrates a possible intermediate in the base-flipping pathway. (3) The orphaned Thy residue displays structural flexibility by adopting an extrahelical or intrahelical position where it is in contact to N120.

Structure and substrate recognition of the Escherichia coli DNA adenine methyltransferase.,Horton JR, Liebert K, Bekes M, Jeltsch A, Cheng X J Mol Biol. 2006 Apr 28;358(2):559-70. Epub 2006 Feb 28. PMID:16524590^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Horton JR, Liebert K, Bekes M, Jeltsch A, Cheng X. Structure and substrate recognition of the Escherichia coli DNA adenine methyltransferase. J Mol Biol. 2006 Apr 28;358(2):559-70. Epub 2006 Feb 28. PMID:16524590 doi:10.1016/j.jmb.2006.02.028

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2g1p"

@@ Line 1: / Line 1: @@
 ==Structure of E. coli DNA adenine methyltransferase (DAM)==
 <StructureSection load='2g1p' size='340' side='right' caption='[[2g1p]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dam ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </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=2g1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g1p OCA], [http://pdbe.org/2g1p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2g1p RCSB], [http://www.ebi.ac.uk/pdbsum/2g1p PDBsum]</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=2g1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g1p OCA], [http://pdbe.org/2g1p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2g1p RCSB], [http://www.ebi.ac.uk/pdbsum/2g1p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2g1p ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 15: / Line 16: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g1/2g1p_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g1/2g1p_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

2g1p

From Proteopedia

Revision as of 06:55, 20 June 2018

Structure of E. coli DNA adenine methyltransferase (DAM)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox