3kcc

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[[Image:3kcc.png|left|200px]]
 
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==Crystal structure of D138L mutant of Catabolite Gene Activator Protein==
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The line below this paragraph, containing "STRUCTURE_3kcc", creates the "Structure Box" on the page.
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<StructureSection load='3kcc' size='340' side='right'caption='[[3kcc]], [[Resolution|resolution]] 1.66&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3kcc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KCC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KCC FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.66&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMP:ADENOSINE-3,5-CYCLIC-MONOPHOSPHATE'>CMP</scene></td></tr>
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{{STRUCTURE_3kcc| PDB=3kcc | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3kcc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kcc OCA], [https://pdbe.org/3kcc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kcc RCSB], [https://www.ebi.ac.uk/pdbsum/3kcc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kcc ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CRP_ECOLI CRP_ECOLI] This protein complexes with cyclic AMP and binds to specific DNA sites near the promoter to regulate the transcription of several catabolite-sensitive operons. The protein induces a severe bend in the DNA. Acts as a negative regulator of its own synthesis as well as for adenylate cyclase (cyaA), which generates cAMP.<ref>PMID:2982847</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kc/3kcc_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3kcc ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The X-ray crystal structure of the cAMP-liganded D138L mutant of Escherichia coli catabolite gene activator protein (CAP) was determined at a resolution of 1.66A. This high resolution crystal structure reveals four cAMP binding sites in the homodimer. Two anti conformations of cAMPs (anti-cAMP) locate between the beta-barrel and the C-helix of each subunit; two syn conformations of cAMPs (syn-cAMP) bind on the surface of the C-terminal domain. With two syn-cAMP molecules bound, the D138L CAP is highly symmetrical with both subunits assuming a "closed" conformation. These differences make the hinge region of the mutant more flexible. Protease susceptibility measurements indicate that D138L is more susceptible to proteases than that of wild type (WT) CAP. The results of protein dynamic experiments (H/D exchange measurements) indicate that the structure of D138L mutant is more dynamic than that of WT CAP, which may impact the recognition of specific DNA sequences.
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===Crystal structure of D138L mutant of Catabolite Gene Activator Protein===
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The 1.6A resolution structure of activated D138L mutant of catabolite gene activator protein with two cAMP bound in each monomer.,Tao W, Gao Z, Gao Z, Zhou J, Huang Z, Dong Y, Yu S Int J Biol Macromol. 2011 Apr 1;48(3):459-65. Epub 2011 Jan 19. PMID:21255606<ref>PMID:21255606</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3kcc" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_21255606}}, adds the Publication Abstract to the page
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*[[Catabolite gene activator protein 3D structures|Catabolite gene activator protein 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 21255606 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_21255606}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Escherichia coli K-12]]
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[[3kcc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KCC OCA].
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[[Category: Large Structures]]
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[[Category: Dong YH]]
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==Reference==
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[[Category: Gao ZQ]]
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<ref group="xtra">PMID:021255606</ref><references group="xtra"/>
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[[Category: Tao WB]]
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[[Category: Escherichia coli]]
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[[Category: Yu SN]]
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[[Category: Dong, Y H.]]
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[[Category: Zhou JH]]
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[[Category: Gao, Z Q.]]
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[[Category: Tao, W B.]]
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[[Category: Yu, S N.]]
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[[Category: Zhou, J H.]]
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[[Category: Activator]]
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[[Category: Camp]]
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[[Category: Camp-binding]]
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[[Category: Dna-binding]]
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[[Category: Helix-turn-helix]]
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[[Category: Nucleotide-binding]]
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[[Category: Transcription]]
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[[Category: Transcription regulation]]
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Current revision

Crystal structure of D138L mutant of Catabolite Gene Activator Protein

PDB ID 3kcc

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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