1mt5: Difference between revisions

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<StructureSection load='1mt5' size='340' side='right'caption='[[1mt5]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='1mt5' size='340' side='right'caption='[[1mt5]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1mt5]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. 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 [http://proteopedia.org/fgij/fg.htm?mol=1MT5 FirstGlance]. <br>
<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='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>
</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FAAH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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'>[http://proteopedia.org/fgij/fg.htm?mol=1mt5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mt5 OCA], [http://pdbe.org/1mt5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mt5 RCSB], [http://www.ebi.ac.uk/pdbsum/1mt5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mt5 ProSAT]</span></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>
</table>
== Function ==
== Function ==
[[http://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).  
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1mt5 ConSurf].
</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="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.
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>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1mt5" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Fatty acid amide hydrolase|Fatty acid amide hydrolase]]
*[[Fatty acid amide hydrolase|Fatty acid amide hydrolase]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Buffalo rat]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bracey, M H]]
[[Category: Rattus norvegicus]]
[[Category: Cravatt, B F]]
[[Category: Bracey MH]]
[[Category: Hanson, M A]]
[[Category: Cravatt BF]]
[[Category: Masuda, K R]]
[[Category: Hanson MA]]
[[Category: Stevens, R C]]
[[Category: Masuda KR]]
[[Category: Amidase signature]]
[[Category: Stevens RC]]
[[Category: Hydrolase]]

Revision as of 09:07, 3 April 2024

CRYSTAL STRUCTURE OF FATTY ACID AMIDE HYDROLASECRYSTAL STRUCTURE OF FATTY ACID AMIDE HYDROLASE

Structural highlights

1mt5 is a 16 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.8Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1mt5, resolution 2.80Å

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