3whc: Difference between revisions
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{{STRUCTURE_3whc| PDB=3whc | SCENE= }} | |||
===Crystal structure of a transcriptional regulator FadR from Bacillus subtilis in complex with stearoyl-CoA=== | |||
{{ABSTRACT_PUBMED_24356978}} | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/FADR_BACSU FADR_BACSU]] Transcriptional regulator in fatty acid degradation. Represses transcription of genes required for fatty acid transport and beta-oxidation, including acdA, fadA, fadB, fadE, fadF, fadG, fadH, fadM, fadN, lcfA and lcfB. Binding of FadR to DNA is specifically inhibited by long chain fatty acyl-CoA compounds of 14-20 carbon atoms in length. | |||
==About this Structure== | |||
[[3whc]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WHC OCA]. | |||
==Reference== | |||
<ref group="xtra">PMID:024356978</ref><references group="xtra"/><references/> | |||
[[Category: Fujihashi, M.]] | |||
[[Category: Miki, K.]] | |||
[[Category: Nakatani, T.]] | |||
[[Category: Fatty acid degradation]] | |||
[[Category: Transcription]] | |||
[[Category: Transcriptional regulator]] | |||
Revision as of 08:58, 19 March 2014
Crystal structure of a transcriptional regulator FadR from Bacillus subtilis in complex with stearoyl-CoA
Template:ABSTRACT PUBMED 24356978
Function
[FADR_BACSU] Transcriptional regulator in fatty acid degradation. Represses transcription of genes required for fatty acid transport and beta-oxidation, including acdA, fadA, fadB, fadE, fadF, fadG, fadH, fadM, fadN, lcfA and lcfB. Binding of FadR to DNA is specifically inhibited by long chain fatty acyl-CoA compounds of 14-20 carbon atoms in length.
About this Structure
3whc is a 6 chain structure. Full crystallographic information is available from OCA.
Reference
- Fujihashi M, Nakatani T, Hirooka K, Matsuoka H, Fujita Y, Miki K. Structural characterization of a ligand-bound form of Bacillus subtilis FadR involved in the regulation of fatty acid degradation. Proteins. 2013 Dec 20. doi: 10.1002/prot.24496. PMID:24356978 doi:https://dx.doi.org/10.1002/prot.24496
