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New page: left|200px<br /><applet load="1fjr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fjr, resolution 2.30Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1fjr.jpg|left|200px]]<br /><applet load="1fjr" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1fjr, resolution 2.30&Aring;" />
'''CRYSTAL STRUCTURE OF THE ECTODOMAIN OF METHUSELAH'''<br />


==Overview==
==CRYSTAL STRUCTURE OF THE ECTODOMAIN OF METHUSELAH==
The Drosophila mutant methuselah (mth) was identified from a screen for, single gene mutations that extended average lifespan. Mth mutants have a, 35% increase in average lifespan and increased resistance to several forms, of stress, including heat, starvation, and oxidative damage. The protein, affected by this mutation is related to G protein-coupled receptors of the, secretin receptor family. Mth, like secretin receptor family members, has, a large N-terminal ectodomain, which may constitute the ligand binding, site. Here we report the 2.3-A resolution crystal structure of the Mth, extracellular region, revealing a folding topology in which three, primarily beta-structure-containing domains meet to form a shallow, interdomain groove containing a solvent-exposed tryptophan that may, represent a ligand binding site. The Mth structure is analyzed in relation, to predicted Mth homologs and potential ligand binding features.
<StructureSection load='1fjr' size='340' side='right'caption='[[1fjr]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1fjr]] 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=1FJR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FJR FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PB:LEAD+(II)+ION'>PB</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fjr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fjr OCA], [https://pdbe.org/1fjr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fjr RCSB], [https://www.ebi.ac.uk/pdbsum/1fjr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fjr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MTH_DROME MTH_DROME] Involved in biological aging and stress response. Essential for adult survival. Required in the presynaptic motor neuron to up-regulate neurotransmitter exocytosis at larval glutamatergic neuromuscular junctions (NMJs). Regulates a step associated with docking and clustering of vesicles at release sites. Sun, Acp70A/SP and eys/SPAM are agonists that activate mth.<ref>PMID:9794765</ref> <ref>PMID:12367510</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fj/1fjr_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1fjr ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Drosophila mutant methuselah (mth) was identified from a screen for single gene mutations that extended average lifespan. Mth mutants have a 35% increase in average lifespan and increased resistance to several forms of stress, including heat, starvation, and oxidative damage. The protein affected by this mutation is related to G protein-coupled receptors of the secretin receptor family. Mth, like secretin receptor family members, has a large N-terminal ectodomain, which may constitute the ligand binding site. Here we report the 2.3-A resolution crystal structure of the Mth extracellular region, revealing a folding topology in which three primarily beta-structure-containing domains meet to form a shallow interdomain groove containing a solvent-exposed tryptophan that may represent a ligand binding site. The Mth structure is analyzed in relation to predicted Mth homologs and potential ligand binding features.


==About this Structure==
Crystal structure of the ectodomain of Methuselah, a Drosophila G protein-coupled receptor associated with extended lifespan.,West AP Jr, Llamas LL, Snow PM, Benzer S, Bjorkman PJ Proc Natl Acad Sci U S A. 2001 Mar 27;98(7):3744-9. Epub 2001 Mar 13. PMID:11274391<ref>PMID:11274391</ref>
1FJR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with NAG, SO4 and PB as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FJR OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Crystal structure of the ectodomain of Methuselah, a Drosophila G protein-coupled receptor associated with extended lifespan., West AP Jr, Llamas LL, Snow PM, Benzer S, Bjorkman PJ, Proc Natl Acad Sci U S A. 2001 Mar 27;98(7):3744-9. Epub 2001 Mar 13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11274391 11274391]
</div>
<div class="pdbe-citations 1fjr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Benzer, S.]]
[[Category: Benzer S]]
[[Category: Bjorkman, P.J.]]
[[Category: Bjorkman PJ]]
[[Category: Jr., A.P.West.]]
[[Category: Llamas LL]]
[[Category: Llamas, L.L.]]
[[Category: Snow PM]]
[[Category: Snow, P.M.]]
[[Category: West Jr AP]]
[[Category: NAG]]
[[Category: PB]]
[[Category: SO4]]
[[Category: ectodomain]]
[[Category: g protein-coupled receptor]]
[[Category: gpcr]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:59:08 2007''

Latest revision as of 04:31, 17 October 2024

CRYSTAL STRUCTURE OF THE ECTODOMAIN OF METHUSELAH

1fjr, resolution 2.30Å

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