1wa9

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[[Image:1wa9.gif|left|200px]]<br /><applet load="1wa9" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1wa9, resolution 3.15&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE PAS REPEAT REGION OF THE DROSOPHILA CLOCK PROTEIN PERIOD'''<br />
 
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==Overview==
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==Crystal Structure of the PAS repeat region of the Drosophila clock protein PERIOD==
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<StructureSection load='1wa9' size='340' side='right'caption='[[1wa9]], [[Resolution|resolution]] 3.15&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1wa9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WA9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WA9 FirstGlance]. <br>
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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]] 3.15&#8491;</td></tr>
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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=1wa9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wa9 OCA], [https://pdbe.org/1wa9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wa9 RCSB], [https://www.ebi.ac.uk/pdbsum/1wa9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wa9 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PER_DROME PER_DROME] Essential for biological clock functions. Determines the period length of circadian and ultradian rhythms; an increase in PER dosage leads to shortened circadian rhythms and a decrease leads to lengthened circadian rhythms. Essential for the circadian rhythmicity of locomotor activity, eclosion behavior, and for the rhythmic component of the male courtship song that originates in the thoracic nervous system. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition.
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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/wa/1wa9_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1wa9 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 ==
PERIOD proteins are central components of the Drosophila and mammalian circadian clock. Their function is controlled by daily changes in synthesis, cellular localization, phosphorylation, degradation, as well as specific interactions with other clock components. Here we present the crystal structure of a Drosophila PERIOD (dPER) fragment comprising two tandemly organized PAS (PER-ARNT-SIM) domains (PAS-A and PAS-B) and two additional C-terminal alpha helices (alphaE and alphaF). Our analysis reveals a noncrystallographic dPER dimer mediated by intermolecular interactions of PAS-A with PAS-B and helix alphaF. We show that alphaF is essential for dPER homodimerization and that the PAS-A-alphaF interaction plays a crucial role in dPER clock function, as it is affected by the 29 hr long-period perL mutation.
PERIOD proteins are central components of the Drosophila and mammalian circadian clock. Their function is controlled by daily changes in synthesis, cellular localization, phosphorylation, degradation, as well as specific interactions with other clock components. Here we present the crystal structure of a Drosophila PERIOD (dPER) fragment comprising two tandemly organized PAS (PER-ARNT-SIM) domains (PAS-A and PAS-B) and two additional C-terminal alpha helices (alphaE and alphaF). Our analysis reveals a noncrystallographic dPER dimer mediated by intermolecular interactions of PAS-A with PAS-B and helix alphaF. We show that alphaF is essential for dPER homodimerization and that the PAS-A-alphaF interaction plays a crucial role in dPER clock function, as it is affected by the 29 hr long-period perL mutation.
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==About this Structure==
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Crystal structure and interactions of the PAS repeat region of the Drosophila clock protein PERIOD.,Yildiz O, Doi M, Yujnovsky I, Cardone L, Berndt A, Hennig S, Schulze S, Urbanke C, Sassone-Corsi P, Wolf E Mol Cell. 2005 Jan 7;17(1):69-82. PMID:15629718<ref>PMID:15629718</ref>
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1WA9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WA9 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Crystal structure and interactions of the PAS repeat region of the Drosophila clock protein PERIOD., Yildiz O, Doi M, Yujnovsky I, Cardone L, Berndt A, Hennig S, Schulze S, Urbanke C, Sassone-Corsi P, Wolf E, Mol Cell. 2005 Jan 7;17(1):69-82. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15629718 15629718]
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</div>
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[[Category: Drosophila melanogaster]]
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<div class="pdbe-citations 1wa9" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Berndt, A.]]
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[[Category: Cardone, L.]]
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[[Category: Doi, M.]]
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[[Category: Hennig, S.]]
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[[Category: Sassone-Corsi, P.]]
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[[Category: Schulze, S.]]
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[[Category: Urbanke, C.]]
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[[Category: Wolf, E.]]
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[[Category: Yildiz, O.]]
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[[Category: Yujnovsky, I.]]
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[[Category: circadian rhythm]]
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[[Category: clock protein]]
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[[Category: pas domain]]
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[[Category: period]]
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[[Category: phosphorylation]]
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[[Category: polymorphism]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:42:08 2008''
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==See Also==
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*[[Period circadian protein|Period circadian protein]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Drosophila melanogaster]]
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[[Category: Large Structures]]
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[[Category: Berndt A]]
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[[Category: Cardone L]]
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[[Category: Doi M]]
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[[Category: Hennig S]]
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[[Category: Sassone-Corsi P]]
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[[Category: Schulze S]]
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[[Category: Urbanke C]]
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[[Category: Wolf E]]
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[[Category: Yildiz O]]
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[[Category: Yujnovsky I]]

Current revision

Crystal Structure of the PAS repeat region of the Drosophila clock protein PERIOD

PDB ID 1wa9

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