3kcc

From Proteopedia

(Difference between revisions)

Revision as of 09:08, 26 December 2018

Crystal structure of D138L mutant of Catabolite Gene Activator Protein

Structural highlights

3kcc is a 2 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	crp (ECOLI)
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

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.

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^[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
↑ Tao W, Gao Z, Gao Z, Zhou J, Huang Z, Dong Y, Yu S. The 1.6A resolution structure of activated D138L mutant of catabolite gene activator protein with two cAMP bound in each monomer. Int J Biol Macromol. 2011 Apr 1;48(3):459-65. Epub 2011 Jan 19. PMID:21255606 doi:10.1016/j.ijbiomac.2011.01.009

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3kcc"

@@ Line 1: / Line 1: @@
 ==Crystal structure of D138L mutant of Catabolite Gene Activator Protein==
 <StructureSection load='3kcc' size='340' side='right' caption='[[3kcc]], [[Resolution|resolution]] 1.66&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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">crp ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=3kcc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kcc OCA], [http://pdbe.org/3kcc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3kcc RCSB], [http://www.ebi.ac.uk/pdbsum/3kcc 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=3kcc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kcc OCA], [http://pdbe.org/3kcc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3kcc RCSB], [http://www.ebi.ac.uk/pdbsum/3kcc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3kcc 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/kc/3kcc_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kc/3kcc_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

3kcc

From Proteopedia

Revision as of 09:08, 26 December 2018

Crystal structure of D138L mutant of Catabolite Gene Activator Protein

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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