1yf2
From Proteopedia
(Difference between revisions)
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<StructureSection load='1yf2' size='340' side='right' caption='[[1yf2]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='1yf2' size='340' side='right' caption='[[1yf2]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1yf2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1yf2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Metja Metja]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YF2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YF2 FirstGlance]. <br> |
| - | </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=1yf2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yf2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1yf2 RCSB], [http://www.ebi.ac.uk/pdbsum/1yf2 PDBsum], [http://www.topsan.org/Proteins/BSGC/1yf2 TOPSAN]</span></td></tr> | + | </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=1yf2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yf2 OCA], [http://pdbe.org/1yf2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yf2 RCSB], [http://www.ebi.ac.uk/pdbsum/1yf2 PDBsum], [http://www.topsan.org/Proteins/BSGC/1yf2 TOPSAN]</span></td></tr> |
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/T1S1_METJA T1S1_METJA]] The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance MTase modifying the DNA so that both strands become methylated. Subunit S dictates DNA sequences specificity (By similarity). | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 1yf2" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Metja]] |
[[Category: Adams, P D]] | [[Category: Adams, P D]] | ||
[[Category: Structural genomic]] | [[Category: Structural genomic]] | ||
Revision as of 22:52, 10 September 2015
Three-dimensional structure of DNA sequence specificity (S) subunit of a type I restriction-modification enzyme and its functional implications
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