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1g6n

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Revision as of 06:46, 3 January 2018

2.1 ANGSTROM STRUCTURE OF CAP-CAMP

Structural highlights

1g6n is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. This structure supersedes the now removed PDB entries 3gap and 1gap. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	3gap
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

After an allosteric transition produced by the binding of cyclic AMP (cAMP), the Escherichia coli catabolite gene activator protein (CAP) binds DNA specifically and activates transcription. The three-dimensional crystal structure of the CAP-cAMP complex has been refined at 2.1 A resolution, thus enabling a better evaluation of the structural basis for CAP phenotypes, the interactions of cAMP with CAP and the roles played by water structure. A review of mutational analysis of CAP together with the additional structural information presented here suggests a possible mechanism for the cAMP-induced allostery required for DNA binding and transcriptional activation. We hypothesize that cAMP binding may reorient the coiled-coil C-helices, which provide most of the dimer interface, thereby altering the relative positions of the DNA-binding domains of the CAP dimer. Additionally, cAMP binding may cause a further rearrangement of the DNA-binding and cAMP-binding domains of CAP via a flap consisting of beta-strands 4 and 5 which lies over the cAMP.

Modeling the cAMP-induced allosteric transition using the crystal structure of CAP-cAMP at 2.1 A resolution.,Passner JM, Schultz SC, Steitz TA J Mol Biol. 2000 Dec 15;304(5):847-59. PMID:11124031^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Aiba H. Transcription of the Escherichia coli adenylate cyclase gene is negatively regulated by cAMP-cAMP receptor protein. J Biol Chem. 1985 Mar 10;260(5):3063-70. PMID:2982847
↑ Passner JM, Schultz SC, Steitz TA. Modeling the cAMP-induced allosteric transition using the crystal structure of CAP-cAMP at 2.1 A resolution. J Mol Biol. 2000 Dec 15;304(5):847-59. PMID:11124031 doi:http://dx.doi.org/10.1006/jmbi.2000.4231

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1g6n"

@@ Line 1: / Line 1: @@
 ==2.1 ANGSTROM STRUCTURE OF CAP-CAMP==
 <StructureSection load='1g6n' size='340' side='right' caption='[[1g6n]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CMP:ADENOSINE-3,5-CYCLIC-MONOPHOSPHATE'>CMP</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3gap|3gap]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g6n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g6n OCA], [http://pdbe.org/1g6n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g6n RCSB], [http://www.ebi.ac.uk/pdbsum/1g6n PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g6n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g6n OCA], [http://pdbe.org/1g6n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g6n RCSB], [http://www.ebi.ac.uk/pdbsum/1g6n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1g6n ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g6/1g6n_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g6/1g6n_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 28: / Line 29: @@
 </div>
 <div class="pdbe-citations 1g6n" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Catabolite gene activator protein|Catabolite gene activator protein]]
 == References ==
 <references/>

1g6n

From Proteopedia

Revision as of 06:46, 3 January 2018

2.1 ANGSTROM STRUCTURE OF CAP-CAMP

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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