This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1ezw

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 07:16, 20 December 2017

STRUCTURE OF COENZYME F420 DEPENDENT TETRAHYDROMETHANOPTERIN REDUCTASE FROM METHANOPYRUS KANDLERI

Structural highlights

1ezw is a 1 chain structure with sequence from Methanopyrus kandleri. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1f07
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MER_METKA] Catalyzes the reversible reduction of methylene-H(4)MPT to methyl-H(4)MPT.[HAMAP-Rule:MF_01091]

Evolutionary Conservation

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

Publication Abstract from PubMed

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.

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:10891279^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Shima S, Warkentin E, Grabarse W, Sordel M, Wicke M, Thauer RK, Ermler U. Structure of coenzyme F(420) dependent methylenetetrahydromethanopterin reductase from two methanogenic archaea. J Mol Biol. 2000 Jul 21;300(4):935-50. PMID:10891279 doi:http://dx.doi.org/10.1006/jmbi.2000.3909

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ezw"

@@ Line 1: / Line 1: @@
 ==STRUCTURE OF COENZYME F420 DEPENDENT TETRAHYDROMETHANOPTERIN REDUCTASE FROM METHANOPYRUS KANDLERI==
 <StructureSection load='1ezw' size='340' side='right' caption='[[1ezw]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1f07|1f07]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ezw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ezw OCA], [http://pdbe.org/1ezw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ezw RCSB], [http://www.ebi.ac.uk/pdbsum/1ezw PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ezw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ezw OCA], [http://pdbe.org/1ezw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ezw RCSB], [http://www.ebi.ac.uk/pdbsum/1ezw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ezw ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ez/1ezw_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ez/1ezw_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1ezw

From Proteopedia

Revision as of 07:16, 20 December 2017

STRUCTURE OF COENZYME F420 DEPENDENT TETRAHYDROMETHANOPTERIN REDUCTASE FROM METHANOPYRUS KANDLERI

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox