View source for 2ydx


==Crystal structure of human S-adenosylmethionine synthetase 2, beta subunit==
<StructureSection load='2ydx' size='340' side='right'caption='[[2ydx]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2ydx]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YDX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YDX 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]] 2.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=STL:RESVERATROL'>STL</scene>, <scene name='pdbligand=TXP:1,4,5,6-TETRAHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE+PHOSPHATE'>TXP</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=2ydx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ydx OCA], [https://pdbe.org/2ydx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ydx RCSB], [https://www.ebi.ac.uk/pdbsum/2ydx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ydx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MAT2B_HUMAN MAT2B_HUMAN] Non-catalytic regulatory subunit of S-adenosylmethionine synthetase 2 (MAT2A), an enzyme that catalyzes the formation of S-adenosylmethionine from methionine and ATP. Regulates the activity of S-adenosylmethionine synthetase 2 by changing its kinetic properties, rendering the enzyme more susceptible to S-adenosylmethionine inhibition.<ref>PMID:10644686</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
MAT (methionine adenosyltransferase) utilizes L-methionine and ATP to form SAM (S-adenosylmethionine), the principal methyl donor in biological methylation. Mammals encode a liver-specific isoenzyme, MAT1A, that is genetically linked with an inborn metabolic disorder of hypermethioninaemia, as well as a ubiquitously expressed isoenzyme, MAT2A, whose enzymatic activity is regulated by an associated subunit MAT2B. To understand the molecular mechanism of MAT functions and interactions, we have crystallized the ligand-bound complexes of human MAT1A, MAT2A and MAT2B. The structures of MAT1A and MAT2A in binary complexes with their product SAM allow for a comparison with the Escherichia coli and rat structures. This facilitates the understanding of the different substrate or product conformations, mediated by the neighbouring gating loop, which can be accommodated by the compact active site during catalysis. The structure of MAT2B reveals an SDR (short-chain dehydrogenase/reductase) core with specificity for the NADP/H cofactor, and harbours the SDR catalytic triad (YxxxKS). Extended from the MAT2B core is a second domain with homology with an SDR sub-family that binds nucleotide-sugar substrates, although the equivalent region in MAT2B presents a more open and extended surface which may endow a different ligand/protein-binding capability. Together, the results of the present study provide a framework to assign structural features to the functional and catalytic properties of the human MAT proteins, and facilitate future studies to probe new catalytic and binding functions.

Insight into S-adenosylmethionine biosynthesis from the crystal structures of the human methionine adenosyltransferase catalytic and regulatory subunits.,Shafqat N, Muniz JR, Pilka ES, Papagrigoriou E, von Delft F, Oppermann U, Yue WW Biochem J. 2013 May 15;452(1):27-36. doi: 10.1042/BJ20121580. PMID:23425511<ref>PMID:23425511</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2ydx" style="background-color:#fffaf0;"></div>

==See Also==
*[[Methionine adenosyltransferase|Methionine adenosyltransferase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Arrowsmith CH]]
[[Category: Bountra C]]
[[Category: Edwards AM]]
[[Category: Gileadi O]]
[[Category: Kavanagh KL]]
[[Category: Muniz JRC]]
[[Category: Oppermann U]]
[[Category: Papagriogriou V]]
[[Category: Pike ACW]]
[[Category: Roos A]]
[[Category: Shafqat N]]
[[Category: Vollmar M]]
[[Category: Weigelt J]]
[[Category: Yue WW]]
[[Category: Von Delft F]]