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==Inter-dimeric interface controls function and stability of S-methionine adenosyltransferase from U. urealiticum==
<StructureSection load='6rk5' size='340' side='right'caption='[[6rk5]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6rk5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Ureaplasma_urealyticum_serovar_7_str._ATCC_27819 Ureaplasma urealyticum serovar 7 str. ATCC 27819]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RK5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RK5 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]] 2.6&#8491;</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=6rk5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rk5 OCA], [https://pdbe.org/6rk5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rk5 RCSB], [https://www.ebi.ac.uk/pdbsum/6rk5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rk5 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Methionine S-adenosyltransferases (MATs) are predominantly homotetramers, comprised of dimers of dimers. The larger, highly conserved intradimeric interface harbors two active sites, making the dimer the obligatory functional unit. However, functionality of the smaller, more diverged, and recently evolved interdimeric interface is largely unknown. Here, we show that the interdimeric interface of Ureaplasmaurealiticum MAT has evolved to control the catalytic activity and structural integrity of the homotetramer in response to product accumulation. When all four active sites are occupied with the product, S-adenosylmethionine (SAM), binding of four additional SAM molecules to the interdimeric interface prompts a approximately 45 degrees shift in the dimer orientation and a concomitant approximately 60% increase in the interface area. This rearrangement inhibits the enzymatic activity by locking the flexible active site loops in a closed state and renders the tetramer resistant to proteolytic degradation. Our findings suggest that the interdimeric interface of MATs is subject to rapid evolutionary changes that tailor the molecular properties of the entire homotetramer to the specific needs of the organism.

The interdimeric interface controls function and stability of Ureaplasma urealiticum methionine S-adenosyltransferase.,Kleiner D, Shmulevich F, Zarivach R, Shahar A, Sharon M, Ben-Nissan G, Bershtein S J Mol Biol. 2019 Dec 6;431(24):4796-4816. doi: 10.1016/j.jmb.2019.09.003. Epub, 2019 Sep 12. PMID:31520601<ref>PMID:31520601</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6rk5" style="background-color:#fffaf0;"></div>

==See Also==
*[[S-adenosylmethionine synthetase 3D structures|S-adenosylmethionine synthetase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Ureaplasma urealyticum serovar 7 str. ATCC 27819]]
[[Category: Bershtein S]]
[[Category: Kleiner D]]
[[Category: Shahar A]]
[[Category: Shmulevich F]]
[[Category: Zarivach R]]