3i59

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{{Seed}}
 
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[[Image:3i59.png|left|200px]]
 
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==Crystal structure of MtbCRP in complex with N6-cAMP==
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The line below this paragraph, containing "STRUCTURE_3i59", creates the "Structure Box" on the page.
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<StructureSection load='3i59' size='340' side='right'caption='[[3i59]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3i59]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3I59 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3I59 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.29&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=N6R:(2R)-N6-(1-METHYL-2-PHENYLETHYL)ADENOSINE-3,5-CYCLIC+MONOPHOSPHATE'>N6R</scene>, <scene name='pdbligand=N6S:(2S)-N6-(1-METHYL-2-PHENYLETHYL)ADENOSINE-3,5-CYCLIC+MONOPHOSPHATE'>N6S</scene></td></tr>
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{{STRUCTURE_3i59| PDB=3i59 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3i59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i59 OCA], [https://pdbe.org/3i59 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3i59 RCSB], [https://www.ebi.ac.uk/pdbsum/3i59 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3i59 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CRPL_MYCTU CRPL_MYCTU] Global transcriptional regulator that complexes with cAMP and binds to specific DNA promoter sites, causing DNA-bending, to regulate transcription. cAMP improves binding to specific DNA sequences, probably by altering protein conformation. The CRP regulon is predicted to contain about 115 genes. Some genes are activated by CRP (rpfA, whiB1) while others are repressed (fadD10). There are 2 CRP-binding sites in the promoter of whiB1, at low concentrations of CRP with or without cAMP transcription of whiB1 is enhanced via site CRP1, then repressed as site CRP2 is filled.<ref>PMID:15882420</ref> <ref>PMID:20028978</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i5/3i59_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=3i59 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The cAMP receptor protein (CRP) from Mycobacterium tuberculosis is a cAMP-responsive global transcriptional regulator, responsible for the regulation of a multitude of diverse proteins. We have determined the crystal structures of the CRP.cAMP and CRP.N(6)-cAMP derivative-bound forms of the enzyme to 2.2- and 2.3 A-resolution, respectively, to investigate cAMP-mediated conformational and structural changes. The allosteric switch from the open, inactive conformation to the closed, active conformation begins with a number of changes in the ligand-binding cavity upon cAMP binding. These subtle structural changes and numerous non-bonding interactions between cAMP, the N-domain residues, and the C-domain helices demonstrate that the N-domain hairpin loop acts as a structural mediator of the allosteric switch. Based on the CRP.N(6)-cAMP crystal structure, binding of N(6)-cAMP with a bulkier methylphenylethyl extension from the N6 atom stabilizes the cAMP-binding domain, N-domain hairpin, and C-terminal domain in a similar manner as that of the CRP.cAMP structure, maintaining structural integrity within the subunits. However, the bulkier N6 extension of N(6)-cAMP (in R conformation) is accommodated only in subunit A with minor changes, whereas in subunit B, the N6 extension is in the S conformation hindering the hinge region of the central helix. As a result, the entire N-domain and the C-domain of subunit B integrated by the cAMP portion of this ligand, together tilt away ( approximately 7 degrees tilt) from central helix C, positioning the helix-turn-helix motif in an unfavorable position for the DNA substrate, asymmetrically. Together, these crystal structures demonstrate the mechanism of action of the cAMP molecule and its role in integrating the active CRP structure.
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===Crystal structure of MtbCRP in complex with N6-cAMP===
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Structural insights into the mechanism of the allosteric transitions of Mycobacterium tuberculosis cAMP receptor protein.,Reddy MC, Palaninathan SK, Bruning JB, Thurman C, Smith D, Sacchettini JC J Biol Chem. 2009 Dec 25;284(52):36581-91. Epub 2009 Sep 9. PMID:19740754<ref>PMID:19740754</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3i59" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_19740754}}, adds the Publication Abstract to the page
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*[[Catabolite gene activator protein 3D structures|Catabolite gene activator protein 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 19740754 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19740754}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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3I59 is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3I59 OCA].
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==Reference==
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<ref group="xtra">PMID:19740754</ref><references group="xtra"/>
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[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
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[[Category: Bruning, J B.]]
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[[Category: Bruning JB]]
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[[Category: Palaninathan, S K.]]
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[[Category: Palaninathan SK]]
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[[Category: Reddy, M C.]]
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[[Category: Reddy MC]]
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[[Category: Sacchettini, J C.]]
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[[Category: Sacchettini JC]]
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[[Category: Smith, D.]]
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[[Category: Smith D]]
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[[Category: TBSGC, TB Structural Genomics Consortium.]]
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[[Category: Thurman C]]
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[[Category: Thurman, C.]]
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[[Category: Allosteric mechanism]]
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[[Category: Camp receptor protein]]
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[[Category: Crp]]
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[[Category: Dna binding]]
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[[Category: Dna binding protein]]
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[[Category: Dna-binding]]
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[[Category: Inhibition]]
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[[Category: Mycobacterium tuberculosis]]
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[[Category: N6-camp]]
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[[Category: Structural genomic]]
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[[Category: Tb structural genomics consortium]]
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[[Category: Tbsgc]]
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[[Category: Transcription]]
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[[Category: Transcription regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 30 14:17:57 2009''
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Current revision

Crystal structure of MtbCRP in complex with N6-cAMP

PDB ID 3i59

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