View source for 5laa


==X-RAY STRUCTURE OF THE METHYLTRANSFERASE SUBUNIT A FROM METHANOTHERMUS FERVIDUS IN COMPLEX WITH COBALAMIN==
<StructureSection load='5laa' size='340' side='right'caption='[[5laa]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5laa]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanothermus_fervidus_DSM_2088 Methanothermus fervidus DSM 2088]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LAA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LAA FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B12:COBALAMIN'>B12</scene></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=5laa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5laa OCA], [https://pdbe.org/5laa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5laa RCSB], [https://www.ebi.ac.uk/pdbsum/5laa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5laa ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/E3GWY7_METFV E3GWY7_METFV] Part of a complex that catalyzes the formation of methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and methyl-tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step.[HAMAP-Rule:MF_01093]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In the three domains of life, vitamin B12 (cobalamin) is primarily used in methyltransferase and isomerase reactions. The methyltransferase complex MtrA-H of methanogenic archaea has a key function in energy conservation by catalysing the methyl transfer from methyl-tetrahydromethanopterin to coenzyme M and its coupling with sodium-ion translocation. The cobalamin-binding subunit MtrA is not homologous to any known B12-binding proteins and is proposed as the motor of the sodium-ion pump. Here, we present crystal structures of the soluble domain of the membrane-associated MtrA from Methanocaldococcus jannaschii and the cytoplasmic MtrA homologue/cobalamin complex from Methanothermus fervidus. The MtrA fold corresponds to the Rossmann-type alpha/beta fold, which is also found in many cobalamin-containing proteins. Surprisingly, the cobalamin-binding site of MtrA differed greatly from all the other cobalamin-binding sites. Nevertheless, the hydrogen-bond linkage at the lower axial-ligand site of cobalt was equivalently constructed to that found in other methyltransferases and mutases. A distinct polypeptide segment fixed through the hydrogen-bond linkage in the relaxed Co(III) state might be involved in propagating the energy released upon corrinoid demethylation to the sodium-translocation site by a conformational change.

MtrA of the sodium ion pumping methyltransferase binds cobalamin in a unique mode.,Wagner T, Ermler U, Shima S Sci Rep. 2016 Jun 21;6:28226. doi: 10.1038/srep28226. PMID:27324530<ref>PMID:27324530</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5laa" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Methanothermus fervidus DSM 2088]]
[[Category: Ermler U]]
[[Category: Shima S]]
[[Category: Wagner T]]