2cgp: Difference between revisions

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-[[Image:2cgp.gif|left|200px]]
- {{Structure
+==CATABOLITE GENE ACTIVATOR PROTEIN/DNA COMPLEX, ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE==
-|PDB= 2cgp |SIZE=350|CAPTION= <scene name='initialview01'>2cgp</scene>, resolution 2.200&Aring;
+<StructureSection load='2cgp' size='340' side='right'caption='[[2cgp]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=CMP:ADENOSINE-3&#39;,5&#39;-CYCLIC-MONOPHOSPHATE'>CMP</scene>
+<table><tr><td colspan='2'>[[2cgp]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CGP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CGP FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
-|GENE=
+<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>
-}}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2cgp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cgp OCA], [https://pdbe.org/2cgp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cgp RCSB], [https://www.ebi.ac.uk/pdbsum/2cgp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cgp ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cg/2cgp_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=2cgp ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The 2.2 A resolution crystal structure of the Escherichia coli catabolite gene activator protein (CAP) complexed with cAMP and a 46-bp DNA fragment reveals a second cAMP molecule bound to each protein monomer. The second cAMP is in the syn conformation and is located on the DNA binding domain interacting with the helix-turn-helix, a beta-hairpin from the regulatory domain and the DNA (via water molecules). The presence of this second cAMP site resolves the apparent discrepancy between the NMR and x-ray data on the conformation of cAMP, and explains the cAMP concentration-dependent behaviors of the protein. In addition, this site's close proximity to mutations affecting transcriptional activation and its water-mediated interactions with a DNA recognition residue (E181) and DNA raise the possibility that this site has biological relevance.
-'''CATABOLITE GENE ACTIVATOR PROTEIN/DNA COMPLEX, ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE'''
+The structure of a CAP-DNA complex having two cAMP molecules bound to each monomer.,Passner JM, Steitz TA Proc Natl Acad Sci U S A. 1997 Apr 1;94(7):2843-7. PMID:9096308<ref>PMID:9096308</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2cgp" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-The 2.2 A resolution crystal structure of the Escherichia coli catabolite gene activator protein (CAP) complexed with cAMP and a 46-bp DNA fragment reveals a second cAMP molecule bound to each protein monomer. The second cAMP is in the syn conformation and is located on the DNA binding domain interacting with the helix-turn-helix, a beta-hairpin from the regulatory domain and the DNA (via water molecules). The presence of this second cAMP site resolves the apparent discrepancy between the NMR and x-ray data on the conformation of cAMP, and explains the cAMP concentration-dependent behaviors of the protein. In addition, this site's close proximity to mutations affecting transcriptional activation and its water-mediated interactions with a DNA recognition residue (E181) and DNA raise the possibility that this site has biological relevance.
+*[[Catabolite gene activator protein 3D structures|Catabolite gene activator protein 3D structures]]
+== References ==
-==About this Structure==
+<references/>
-CGP is a [[Single protein]] structure of 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=2CGP OCA].
+__TOC__
+</StructureSection>
-==Reference==
-The structure of a CAP-DNA complex having two cAMP molecules bound to each monomer., Passner JM, Steitz TA, Proc Natl Acad Sci U S A. 1997 Apr 1;94(7):2843-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9096308 9096308]
 [[Category: Escherichia coli]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Passner, J M.]]
+[[Category: Passner JM]]
-[[Category: Steitz, T A.]]
+[[Category: Steitz TA]]
-[[Category: CMP]]
-[[Category: activator]]
-[[Category: camp-binding]]
-[[Category: complex (transcription regulation/dna)]]
-[[Category: dna-binding]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 14:52:10 2008''