View source for 4bhp


==A structural model of CAP mutant (T127L and S128I) in cGMP-bound state==
<StructureSection load='4bhp' size='340' side='right'caption='[[4bhp]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4bhp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BHP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BHP FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=4bhp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bhp OCA], [https://pdbe.org/4bhp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bhp RCSB], [https://www.ebi.ac.uk/pdbsum/4bhp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bhp 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> 
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== Publication Abstract from PubMed ==
The ability to inhibit binding or enzymatic activity is key to preventing aberrant behaviors of proteins. Allosteric inhibition is desirable as it offers several advantages over competitive inhibition, but the mechanisms of action remain poorly understood in most cases. Here we show that allosteric inhibition can be effected by destabilizing a low-populated conformational state that serves as an on-pathway intermediate for ligand binding, without altering the protein's ground-state structure. As standard structural approaches are typically concerned with changes in the ground-state structure of proteins, the presence of such a mechanism can go easily undetected. Our data strongly argue for the routine use of NMR tools suited to detect and characterize transiently formed conformational states in allosteric systems. Structure information on such important intermediates can ultimately result in more efficient design of allosteric inhibitors.

Allosteric inhibition through suppression of transient conformational states.,Tzeng SR, Kalodimos CG Nat Chem Biol. 2013 May 5. doi: 10.1038/nchembio.1250. PMID:23644478<ref>PMID:23644478</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4bhp" style="background-color:#fffaf0;"></div>

==See Also==
*[[Catabolite gene activator protein 3D structures|Catabolite gene activator protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Kalodimos CG]]
[[Category: Tzeng SR]]