1mt5: Difference between revisions

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-[[Image:1mt5.gif|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_1mt5", creates the "Structure Box" on the page.
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-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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-{{STRUCTURE_1mt5|  PDB=1mt5  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF FATTY ACID AMIDE HYDROLASE'''
+==CRYSTAL STRUCTURE OF FATTY ACID AMIDE HYDROLASE==
+<StructureSection load='1mt5' size='340' side='right'caption='[[1mt5]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1mt5]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MT5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MT5 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]] 2.8&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MAY:METHYL+ARACHIDONYL+FLUOROPHOSPHONATE'>MAY</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=1mt5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mt5 OCA], [https://pdbe.org/1mt5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mt5 RCSB], [https://www.ebi.ac.uk/pdbsum/1mt5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mt5 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/FAAH1_RAT FAAH1_RAT] Degrades bioactive fatty acid amides like oleamide, the endogenous cannabinoid, anandamide and myristic amide to their corresponding acids, thereby serving to terminate the signaling functions of these molecules. Hydrolyzes polyunsaturated substrate anandamide preferentially as compared to monounsaturated substrates (By similarity).
+== 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/mt/1mt5_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=1mt5 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Cellular communication in the nervous system is mediated by chemical messengers that include amino acids, monoamines, peptide hormones, and lipids. An interesting question is how neurons regulate signals that are transmitted by membrane-embedded lipids. Here, we report the 2.8 angstrom crystal structure of the integral membrane protein fatty acid amide hydrolase (FAAH), an enzyme that degrades members of the endocannabinoid class of signaling lipids and terminates their activity. The structure of FAAH complexed with an arachidonyl inhibitor reveals how a set of discrete structural alterations allows this enzyme, in contrast to soluble hydrolases of the same family, to integrate into cell membranes and establish direct access to the bilayer from its active site.
-==Overview==
+Structural adaptations in a membrane enzyme that terminates endocannabinoid signaling.,Bracey MH, Hanson MA, Masuda KR, Stevens RC, Cravatt BF Science. 2002 Nov 29;298(5599):1793-6. PMID:12459591<ref>PMID:12459591</ref>
-Cellular communication in the nervous system is mediated by chemical messengers that include amino acids, monoamines, peptide hormones, and lipids. An interesting question is how neurons regulate signals that are transmitted by membrane-embedded lipids. Here, we report the 2.8 angstrom crystal structure of the integral membrane protein fatty acid amide hydrolase (FAAH), an enzyme that degrades members of the endocannabinoid class of signaling lipids and terminates their activity. The structure of FAAH complexed with an arachidonyl inhibitor reveals how a set of discrete structural alterations allows this enzyme, in contrast to soluble hydrolases of the same family, to integrate into cell membranes and establish direct access to the bilayer from its active site.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-MT5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MT5 OCA].
+</div>
+<div class="pdbe-citations 1mt5" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-Structural adaptations in a membrane enzyme that terminates endocannabinoid signaling., Bracey MH, Hanson MA, Masuda KR, Stevens RC, Cravatt BF, Science. 2002 Nov 29;298(5599):1793-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12459591 12459591]
+*[[Fatty acid amide hydrolase|Fatty acid amide hydrolase]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Rattus norvegicus]]
-[[Category: Single protein]]
+[[Category: Bracey MH]]
-[[Category: Bracey, M H.]]
+[[Category: Cravatt BF]]
-[[Category: Cravatt, B F.]]
+[[Category: Hanson MA]]
-[[Category: Hanson, M A.]]
+[[Category: Masuda KR]]
-[[Category: Masuda, K R.]]
+[[Category: Stevens RC]]
-[[Category: Stevens, R C.]]
-[[Category: Amidase signature]]
-[[Category: Hydrolase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 01:41:19 2008''