2dtr
From Proteopedia
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{{STRUCTURE_2dtr| PDB=2dtr | SCENE= }} | {{STRUCTURE_2dtr| PDB=2dtr | SCENE= }} | ||
===STRUCTURE OF DIPHTHERIA TOXIN REPRESSOR=== | ===STRUCTURE OF DIPHTHERIA TOXIN REPRESSOR=== | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | [[2dtr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Corynebacterium_diphtheriae Corynebacterium diphtheriae]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1dtr 1dtr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DTR OCA]. | |
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:008823163</ref><ref group="xtra">PMID:011917145</ref><ref group="xtra">PMID:015048824</ref><references group="xtra"/> |
[[Category: Corynebacterium diphtheriae]] | [[Category: Corynebacterium diphtheriae]] | ||
[[Category: Hol, W G.]] | [[Category: Hol, W G.]] | ||
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[[Category: Repressor]] | [[Category: Repressor]] | ||
[[Category: Transcription regulation]] | [[Category: Transcription regulation]] | ||
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Revision as of 10:24, 6 January 2013
STRUCTURE OF DIPHTHERIA TOXIN REPRESSOR
Template:ABSTRACT PUBMED 8823163
About this Structure
2dtr is a 1 chain structure with sequence from Corynebacterium diphtheriae. This structure supersedes the now removed PDB entry 1dtr. Full crystallographic information is available from OCA.
Reference
- Qiu X, Pohl E, Holmes RK, Hol WG. High-resolution structure of the diphtheria toxin repressor complexed with cobalt and manganese reveals an SH3-like third domain and suggests a possible role of phosphate as co-corepressor. Biochemistry. 1996 Sep 24;35(38):12292-302. PMID:8823163 doi:http://dx.doi.org/10.1021/bi960861d
- Bhattacharyya R, Samanta U, Chakrabarti P. Aromatic-aromatic interactions in and around alpha-helices. Protein Eng. 2002 Feb;15(2):91-100. PMID:11917145
- 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
