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New page: left|200px<br /><applet load="1y5y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y5y, resolution 2.00Å" /> '''Structure of the tet...
 
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[[Image:1y5y.gif|left|200px]]<br /><applet load="1y5y" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1y5y, resolution 2.00&Aring;" />
'''Structure of the tetrahydromethanopterin dependent formaldehyde-activating enzyme (Fae) from Methylobacterium extorquens AM1'''<br />


==Overview==
==Structure of the tetrahydromethanopterin dependent formaldehyde-activating enzyme (Fae) from Methylobacterium extorquens AM1==
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.
<StructureSection load='1y5y' size='340' side='right'caption='[[1y5y]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<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>
1Y5Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methylobacterium_extorquens Methylobacterium extorquens] with CA and NA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Y5Y OCA].  
</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>
 
<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>
==Reference==
<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>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=15632161 15632161]
</table>
[[Category: Methylobacterium extorquens]]
== Function ==
[[Category: Single protein]]
[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>
[[Category: Acharya, P.]]
== Evolutionary Conservation ==
[[Category: Demmer, U.]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: Ermler, U.]]
Check<jmol>
[[Category: Goenrich, M.]]
  <jmolCheckbox>
[[Category: Hagemeier, C.H.]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/y5/1y5y_consurf.spt"</scriptWhenChecked>
[[Category: Thauer, R.K.]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
[[Category: Vorholt, J.A.]]
    <text>to colour the structure by Evolutionary Conservation</text>
[[Category: CA]]
  </jmolCheckbox>
[[Category: NA]]
</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].
[[Category: beta-alpha-beta left handed crossover]]
<div style="clear:both"></div>
[[Category: flexible c-terminus]]
== References ==
[[Category: pentamer]]
<references/>
 
__TOC__
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:35:32 2007''
</StructureSection>
[[Category: Large Structures]]
[[Category: Methylorubrum extorquens AM1]]
[[Category: Acharya P]]
[[Category: Demmer U]]
[[Category: Ermler U]]
[[Category: Goenrich M]]
[[Category: Hagemeier CH]]
[[Category: Thauer RK]]
[[Category: Vorholt JA]]

Latest revision as of 08:55, 14 February 2024

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

1y5y, resolution 2.00Å

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