1y5y

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[[Image:1y5y.gif|left|200px]]
 
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{{Structure
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==Structure of the tetrahydromethanopterin dependent formaldehyde-activating enzyme (Fae) from Methylobacterium extorquens AM1==
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|PDB= 1y5y |SIZE=350|CAPTION= <scene name='initialview01'>1y5y</scene>, resolution 2.00&Aring;
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<StructureSection load='1y5y' size='340' side='right'caption='[[1y5y]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=NA:SODIUM ION'>NA</scene>
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<table><tr><td colspan='2'>[[1y5y]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylorubrum_extorquens_AM1 Methylorubrum extorquens AM1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y5Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y5Y FirstGlance]. <br>
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|ACTIVITY=
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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&#8491;</td></tr>
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|GENE= fae ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=408 Methylobacterium extorquens])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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}}
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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=1y5y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y5y OCA], [https://pdbe.org/1y5y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y5y RCSB], [https://www.ebi.ac.uk/pdbsum/1y5y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y5y ProSAT]</span></td></tr>
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</table>
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'''Structure of the tetrahydromethanopterin dependent formaldehyde-activating enzyme (Fae) from Methylobacterium extorquens AM1'''
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== Function ==
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[https://www.uniprot.org/uniprot/FAE_METEA FAE_METEA] Catalyzes the condensation of formaldehyde with tetrahydromethanopterin (H(4)MPT) to 5,10-methylenetetrahydromethanopterin, a reaction which also proceeds spontaneously, but at a lower rate than that of the enzyme-catalyzed reaction. Is an essential enzyme for methylotrophic energy metabolism and formaldehyde detoxification of this bacterium.<ref>PMID:11073907</ref> <ref>PMID:15632161</ref>
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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Tetrahydromethanopterin (H4 MPT) is a tetrahydrofolate analogue involved as a C1 carrier in the metabolism of various groups of microorganisms. How H4MPT is bound to the respective C1 unit converting enzymes remained elusive. We describe here the structure of the homopentameric formaldehyde-activating enzyme (Fae) from Methylobacterium extorquens AM1 established at 2.0 angstrom without and at 1.9 angstrom with methylene-H4MPT bound. Methylene-H4MPT is bound in an "S"-shaped conformation into the cleft formed between two adjacent subunits. Coenzyme binding is accompanied by side chain rearrangements up to 5 angstrom and leads to a rigidification of the C-terminal arm, a formation of a new hydrophobic cluster, and an inversion of the amide side chain of Gln88. Methylene-H4MPT in Fae shows a characteristic kink between the tetrahydropyrazine and the imidazolidine rings of 70 degrees that is more pronounced than that reported for free methylene-H4MPT in solution (50 degrees). Fae is an essential enzyme for energy metabolism and formaldehyde detoxification of this bacterium and catalyzes the formation of methylene-H4MPT from H4MPT and formaldehyde. The molecular mechanism ofthis reaction involving His22 as acid catalyst is discussed.
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Check<jmol>
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<jmolCheckbox>
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==About this Structure==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/y5/1y5y_consurf.spt"</scriptWhenChecked>
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1Y5Y is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Methylobacterium_extorquens Methylobacterium extorquens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y5Y OCA].
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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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==Reference==
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</jmolCheckbox>
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How an enzyme binds the C1 carrier tetrahydromethanopterin. Structure of the tetrahydromethanopterin-dependent formaldehyde-activating enzyme (Fae) from Methylobacterium extorquens AM1., Acharya P, Goenrich M, Hagemeier CH, Demmer U, Vorholt JA, Thauer RK, Ermler U, J Biol Chem. 2005 Apr 8;280(14):13712-9. Epub 2005 Jan 4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15632161 15632161]
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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=1y5y ConSurf].
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[[Category: Methylobacterium extorquens]]
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<div style="clear:both"></div>
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[[Category: Single protein]]
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== References ==
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[[Category: Acharya, P.]]
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<references/>
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[[Category: Demmer, U.]]
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__TOC__
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[[Category: Ermler, U.]]
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</StructureSection>
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[[Category: Goenrich, M.]]
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[[Category: Large Structures]]
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[[Category: Hagemeier, C H.]]
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[[Category: Methylorubrum extorquens AM1]]
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[[Category: Thauer, R K.]]
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[[Category: Acharya P]]
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[[Category: Vorholt, J A.]]
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[[Category: Demmer U]]
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[[Category: CA]]
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[[Category: Ermler U]]
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[[Category: NA]]
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[[Category: Goenrich M]]
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[[Category: beta-alpha-beta left handed crossover]]
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[[Category: Hagemeier CH]]
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[[Category: flexible c-terminus]]
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[[Category: Thauer RK]]
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[[Category: pentamer]]
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[[Category: Vorholt JA]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:18:49 2008''
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Current revision

Structure of the tetrahydromethanopterin dependent formaldehyde-activating enzyme (Fae) from Methylobacterium extorquens AM1

PDB ID 1y5y

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