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3kot
From Proteopedia
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===Structure of the Citrobacter freundii effector binding domain containing three amino acid substitutions: T103V, S221A and Y264F=== | ===Structure of the Citrobacter freundii effector binding domain containing three amino acid substitutions: T103V, S221A and Y264F=== | ||
| + | {{ABSTRACT_PUBMED_20594961}} | ||
| - | + | ==Function== | |
| - | + | [[http://www.uniprot.org/uniprot/AMPR_CITFR AMPR_CITFR]] Regulates the expression of the beta-lactamase gene. Represses cephalosporinase (AmpC) in the presence of beta-lactams and induces it in the absence of them. | |
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==About this Structure== | ==About this Structure== | ||
| - | + | [[3kot]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Citrobacter_freundii Citrobacter freundii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KOT OCA]. | |
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:020594961</ref><references group="xtra"/><references/> |
[[Category: Citrobacter freundii]] | [[Category: Citrobacter freundii]] | ||
[[Category: Balcewich, M D.]] | [[Category: Balcewich, M D.]] | ||
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[[Category: Transcription]] | [[Category: Transcription]] | ||
[[Category: Transcription regulation]] | [[Category: Transcription regulation]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 28 12:00:08 2010'' | ||
Revision as of 02:21, 4 April 2013
Contents |
Structure of the Citrobacter freundii effector binding domain containing three amino acid substitutions: T103V, S221A and Y264F
Template:ABSTRACT PUBMED 20594961
Function
[AMPR_CITFR] Regulates the expression of the beta-lactamase gene. Represses cephalosporinase (AmpC) in the presence of beta-lactams and induces it in the absence of them.
About this Structure
3kot is a 1 chain structure with sequence from Citrobacter freundii. Full crystallographic information is available from OCA.
Reference
- Balcewich MD, Reeve TM, Orlikow EA, Donald LJ, Vocadlo DJ, Mark BL. Crystal structure of the AmpR effector binding domain provides insight into the molecular regulation of inducible ampc beta-lactamase. J Mol Biol. 2010 Jul 30;400(5):998-1010. Epub 2010 May 31. PMID:20594961 doi:10.1016/j.jmb.2010.05.040
