4bhp
From Proteopedia
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==A structural model of CAP mutant (T127L and S128I) in cGMP-bound state== | ==A structural model of CAP mutant (T127L and S128I) in cGMP-bound state== | ||
| - | <StructureSection load='4bhp' size='340' side='right' caption='[[4bhp | + | <StructureSection load='4bhp' size='340' side='right'caption='[[4bhp]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4bhp]] is a 1 chain structure with sequence from [ | + | <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=' | + | </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'>[ | + | <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> | </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> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 4bhp" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
| - | *[[Catabolite gene activator protein|Catabolite gene activator protein]] | + | *[[Catabolite gene activator protein 3D structures|Catabolite gene activator protein 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Escherichia coli]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Kalodimos CG]] |
| - | [[Category: | + | [[Category: Tzeng SR]] |
Current revision
A structural model of CAP mutant (T127L and S128I) in cGMP-bound state
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