2adm: Difference between revisions
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[[Image:2adm.png|left|200px]] | [[Image:2adm.png|left|200px]] | ||
{{STRUCTURE_2adm| PDB=2adm | SCENE= }} | {{STRUCTURE_2adm| PDB=2adm | SCENE= }} | ||
===ADENINE-N6-DNA-METHYLTRANSFERASE TAQI=== | ===ADENINE-N6-DNA-METHYLTRANSFERASE TAQI=== | ||
{{ABSTRACT_PUBMED_8995524}} | {{ABSTRACT_PUBMED_8995524}} | ||
==About this Structure== | ==About this Structure== | ||
[[2adm]] is a 2 chain structure of [[DNA methyltransferase]] with sequence from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1adm 1adm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ADM OCA]. | |||
==See Also== | |||
*[[DNA methyltransferase|DNA methyltransferase]] | |||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <ref group="xtra">PMID:008995524</ref><ref group="xtra">PMID:015048824</ref><references group="xtra"/> | ||
[[Category: Thermus aquaticus]] | [[Category: Thermus aquaticus]] | ||
[[Category: Saenger, W.]] | [[Category: Saenger, W.]] | ||
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[[Category: Restriction system]] | [[Category: Restriction system]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 21:01, 25 July 2012
ADENINE-N6-DNA-METHYLTRANSFERASE TAQI
Template:ABSTRACT PUBMED 8995524
About this Structure
2adm is a 2 chain structure of DNA methyltransferase with sequence from Thermus aquaticus. This structure supersedes the now removed PDB entry 1adm. Full crystallographic information is available from OCA.
See Also
Reference
- Schluckebier G, Kozak M, Bleimling N, Weinhold E, Saenger W. Differential binding of S-adenosylmethionine S-adenosylhomocysteine and Sinefungin to the adenine-specific DNA methyltransferase M.TaqI. J Mol Biol. 1997 Jan 10;265(1):56-67. PMID:8995524 doi:https://dx.doi.org/10.1006/jmbi.1996.0711
- Hicks JM, Hsu VL. The extended left-handed helix: a simple nucleic acid-binding motif. Proteins. 2004 May 1;55(2):330-8. PMID:15048824 doi:10.1002/prot.10630