1f07: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
New page: left|200px<br /><applet load="1f07" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f07, resolution 2.00Å" /> '''STRUCTURE OF COENZYM...
 
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
 
(16 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1f07.gif|left|200px]]<br /><applet load="1f07" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1f07, resolution 2.00&Aring;" />
'''STRUCTURE OF COENZYME F420 DEPENDENT TETRAHYDROMETHANOPTERIN REDUCTASE FROM METHANOBACTERIUM THERMOAUTOTROPHICUM'''<br />


==Overview==
==STRUCTURE OF COENZYME F420 DEPENDENT TETRAHYDROMETHANOPTERIN REDUCTASE FROM METHANOBACTERIUM THERMOAUTOTROPHICUM==
Coenzyme F(420)-dependent methylenetetrahydromethanopterin reductase (Mer), is an enzyme of the Cl metabolism in methanogenic and sulfate reducing, archaea. It is composed of identical 35-40 kDa subunits and lacks a, prosthetic group. The crystal structure of Mer from Methanopyrus kandleri, (kMer) revealed in one crystal form a dimeric and in another a tetrameric, oligomerisation state and that from Methanobacterium thermoautotrophicum, (tMer) a dimeric state. Each monomer is primarily composed of a TIM-barrel, fold enlarged by three insertion regions. Insertion regions 1 and 2, contribute to intersubunit interactions. Insertion regions 2 and 3, together with the C-terminal end of the TIM-barrel core form a cleft where, the binding sites of coenzyme F(420) and methylene-tetrahydromethanopterin, are postulated. Close to the coenzyme F(420)-binding site lies a rarely, observed non-prolyl cis-peptide bond. It is surprising that Mer is, structurally most similar to a bacterial FMN-dependent luciferase which, contains a non-prolyl cis-peptide bond at the equivalent position. The, structure of Mer is also related to that of NADP-dependent FAD-harbouring, methylenetetrahydrofolate reductase (MetF). However, Mer and MetF do not, show sequence similarities although they bind related substrates and, catalyze an analogous reaction.
<StructureSection load='1f07' size='340' side='right'caption='[[1f07]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1f07]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F07 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F07 FirstGlance]. <br>
1F07 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus] with CL, MPO and MPD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1F07 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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MPO:3[N-MORPHOLINO]PROPANE+SULFONIC+ACID'>MPO</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=1f07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f07 OCA], [https://pdbe.org/1f07 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f07 RCSB], [https://www.ebi.ac.uk/pdbsum/1f07 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f07 ProSAT]</span></td></tr>
Structure of coenzyme F(420) dependent methylenetetrahydromethanopterin reductase from two methanogenic archaea., Shima S, Warkentin E, Grabarse W, Sordel M, Wicke M, Thauer RK, Ermler U, J Mol Biol. 2000 Jul 21;300(4):935-50. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10891279 10891279]
</table>
== Function ==
[https://www.uniprot.org/uniprot/MER_METTM MER_METTM] Catalyzes the reversible reduction of methylene-H(4)MPT to methyl-H(4)MPT.
== 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/f0/1f07_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1f07 ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Methanothermobacter thermautotrophicus]]
[[Category: Methanothermobacter thermautotrophicus]]
[[Category: Single protein]]
[[Category: Ermler U]]
[[Category: Ermler, U.]]
[[Category: Grabarse W]]
[[Category: Grabarse, W.]]
[[Category: Shima S]]
[[Category: Shima, S.]]
[[Category: Thauer RK]]
[[Category: Thauer, R.K.]]
[[Category: Warkentin E]]
[[Category: Warkentin, E.]]
[[Category: CL]]
[[Category: MPD]]
[[Category: MPO]]
[[Category: (beta]]
[[Category: alpha)8 barrel]]
[[Category: tim barrel]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:29:25 2007''
Retrieved from "https://proteopedia.org/1f07"