View source for 5von


==Methionine synthase folate-binding domain from Thermus thermophilus HB8==
<StructureSection load='5von' size='340' side='right'caption='[[5von]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5von]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VON OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VON 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]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=5von FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5von OCA], [https://pdbe.org/5von PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5von RCSB], [https://www.ebi.ac.uk/pdbsum/5von PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5von ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q5SKM5_THET8 Q5SKM5_THET8] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Methyl transfer between methyltetrahydrofolate and corrinoid molecules is a key reaction in biology that is catalyzed by a number of enzymes in many prokaryotic and eukaryotic organisms. One classic example of such an enzyme is cobalamin-dependent methionine synthase (MS). MS is a large modular protein that utilizes an SN2-type mechanism to catalyze the chemically challenging methyl transfer from the tertiary amine (N5) of methyltetrahydrofolate to homocysteine in order to form methionine. Despite over half a century of study, many questions remain about how folate-dependent methyltransferases, and MS in particular, function. Here, the structure of the folate-binding (Fol) domain of MS from Thermus thermophilus is reported in the presence and absence of methyltetrahydrofolate. It is found that the methyltetrahydrofolate-binding environment is similar to those of previously described methyltransferases, highlighting the conserved role of this domain in binding, and perhaps activating, the methyltetrahydrofolate substrate. These structural studies further reveal a new distinct and uncharacterized topology in the C-terminal region of MS Fol domains. Furthermore, it is found that in contrast to the canonical TIM-barrel beta8alpha8 fold found in all other folate-binding domains, MS Fol domains exhibit a unique beta8alpha7 fold. It is posited that these structural differences are important for MS function.

The folate-binding module of Thermus thermophilus cobalamin-dependent methionine synthase displays a distinct variation of the classical TIM barrel: a TIM barrel with a `twist'.,Yamada K, Koutmos M Acta Crystallogr D Struct Biol. 2018 Jan 1;74(Pt 1):41-51. doi:, 10.1107/S2059798317018290. Epub 2018 Jan 1. PMID:29372898<ref>PMID:29372898</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5von" style="background-color:#fffaf0;"></div>

==See Also==
*[[Methionine synthase 3D structures|Methionine synthase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermus thermophilus HB8]]
[[Category: Koutmos M]]
[[Category: Yamada K]]