Catabolite gene activator protein

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<StructureSection load='1o3r' size='350' side='right' scene='54/543372/Cv/3' caption='Catabolite gene activator protein complex with cAMP (stick model) and DNA [[1o3r]]'>
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<StructureSection load='1o3r' size='350' side='right' scene='54/543372/Cv/3' caption='Catabolite gene activator protein complex with cAMP and DNA ([[1o3r]])'>
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'''Catabolite gene activator protein''' (CAP) is a DNA-binding protein involved in the transcription of several genes including those involved in the metabolism of sugar. CAP can activate or repress transcription initiation upon binding of cAMP. The cAMP-CAP complex binds to promoters on the DNA. The structure contains a ligand-binding domain (LBD) at the N-terminal and DNA-binding domain (DBD) at the C-terminal. <scene name='54/543372/Cv/4'>Four cAMP molecules bind to the dimeric CAP</scene>. When the amount of glucose transported into the cell is low, cAMP level rises and the cAMP-CAP complex causes increase of transcription of glucose metabolism genes.<ref>PMID:10550204</ref>
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'''Catabolite gene activator protein''' (CAP) is a DNA-binding protein involved in the transcription of several genes including those involved in the metabolism of sugar. CAP can activate or repress transcription initiation upon binding of cAMP. The cAMP-CAP complex binds to promoters on the DNA. The structure contains a ligand-binding domain (LBD) at the N-terminal and DNA-binding domain (DBD) at the C-terminal. <scene name='54/543372/Cv/4'>Four cAMP molecules bind to the dimeric CAP</scene>. When the amount of glucose transported into the cell is low, cAMP level rises and the cAMP-CAP complex causes increase of transcription of glucose metabolism genes. <ref>PMID:10550204</ref>
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See also [[CAMP-dependent pathway]] and [[CAMP is second messenger]].
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</StructureSection>
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<scene name='54/543372/Cv/11'>1st cAMP binding site</scene>
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== 3D Structures of catabolite gene activator protein ==
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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<scene name='54/543372/Cv/12'>2nd cAMP binding site</scene> in ''E. coli'' Catabolite gene activator protein ([[1o3r]]). <ref>PMID:11724532</ref> Water molecules are shown as red spheres.
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{{#tree:id=OrganizedByTopic|openlevels=0|
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*CAP
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== 3D Structures of catabolite gene activator protein ==
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[[Catabolite gene activator protein 3D structures]]
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**[[3d0s]] – MtCAP – ''Mycobacterium tuberculosis'' <br />
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</StructureSection>
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**[[2wc2]] – EcCAP – ''Escherichia coli'' - NMR<br />
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**[[3hif]], [[4ft8]], [[4hzf]], [[4n9h]] – EcCAP <br />
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**[[3fwe]], [[4bh9]], [[4bhp]] – EcCAP (mutant) <br />
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*CAP complex with cAMP
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**[[1g6n]], [[1i5z]], [[2gzw]], [[3ryp]], [[3ryr]], [[4i01]], [[4i02]], [[4i09]], [[4i0a]], [[4i0b]] – EcCAP + cAMP <br />
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**[[1hw5]], [[1i6x]], [[3kcc]], [[3qop]], [[3rdi]], [[3rou]], [[3rpq]] – EcCAP (mutant) + cAMP <br />
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**[[3i54]], [[3i59]] – MtCAP + cAMP <br />
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*CAP complex with cGMP
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**[[4n9i]] – EcCAP + cGMP <br />
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*CAP complex with cAMP and DNA
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**[[1cgp]], [[1run]], [[2cgp]], [[1j59]], [[1o3q]], [[1o3r]], [[1o3s]], [[1o3t]], [[1zrc]], [[1zrd]], [[1zre]], [[1zrf]] – EcCAP + cAMP + DNA <br />
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**[[1ruo]] – EcCAP (mutant) + cAMP + DNA <br />
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*CAP complex with cAMP, DNA and DNA directed polymerase
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**[[1lb2]], [[3n4m]] – EcCAP + cAMP + DNA + DNA-directed RNA polymerase α subunit<br />
 
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**[[3iyd]] – EcCAP + cAMP + DNA + DNA-directed RNA polymerase α, β, ω subunits + RNA polymerase σ factor – Cryo EM<br />
 
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}}
 
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Catabolite gene activator protein complex with cAMP and DNA (1o3r)

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References

  1. Busby S, Ebright RH. Transcription activation by catabolite activator protein (CAP). J Mol Biol. 1999 Oct 22;293(2):199-213. PMID:10550204 doi:http://dx.doi.org/10.1006/jmbi.1999.3161
  2. Chen S, Vojtechovsky J, Parkinson GN, Ebright RH, Berman HM. Indirect readout of DNA sequence at the primary-kink site in the CAP-DNA complex: DNA binding specificity based on energetics of DNA kinking. J Mol Biol. 2001 Nov 16;314(1):63-74. PMID:11724532 doi:10.1006/jmbi.2001.5089

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Alexander Berchansky, Michal Harel, Jaime Prilusky

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