View source for 6mtg


==A Single Reactive Noncanonical Amino Acid is Able to Dramatically Stabilize Protein Structure==
<StructureSection load='6mtg' size='340' side='right'caption='[[6mtg]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6mtg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MTG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MTG 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]] 1.85&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=6mtg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mtg OCA], [https://pdbe.org/6mtg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mtg RCSB], [https://www.ebi.ac.uk/pdbsum/6mtg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mtg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/METAS_ECOLI METAS_ECOLI] Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine (PubMed:10572016, PubMed:17442255, PubMed:17302437, PubMed:28581482). Utilizes a ping-pong kinetic mechanism in which the succinyl group of succinyl-CoA is initially transferred to the enzyme to form a succinyl-enzyme intermediate before subsequent transfer to homoserine to form the final product, O-succinylhomoserine (PubMed:10572016, PubMed:17442255, PubMed:17302437). Cannot use acetyl-CoA (PubMed:10572016).<ref>PMID:10572016</ref> <ref>PMID:17302437</ref> <ref>PMID:17442255</ref> <ref>PMID:28581482</ref> 
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== Publication Abstract from PubMed ==
A p-isothiocyanate phenylalanine mutant of the homodimeric protein homoserine o-succinyltransferase (MetA) was isolated in a temperature dependent selection from a library of metA mutants containing noncanonical amino acids. This mutant protein has a dramatic increase of 24 degrees C in thermal stability compared to the wild type protein. Peptide mapping experiments revealed that the isothiocyanate group forms a thiourea cross-link to the N terminal proline of the other monomer, despite the two positions being &gt;30 A apart in the X-ray crystal structure of the wild type protein. These results show that an expanded set of building blocks beyond the canonical 20 amino acids can lead to significant changes in the properties of proteins.

A Single Reactive Noncanonical Amino Acid Is Able to Dramatically Stabilize Protein Structure.,Li JC, Nastertorabi F, Xuan W, Han GW, Stevens RC, Schultz PG ACS Chem Biol. 2019 Jun 4. doi: 10.1021/acschembio.9b00002. PMID:31181898<ref>PMID:31181898</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6mtg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Han GW]]
[[Category: Li JC]]
[[Category: Nasertorabi F]]
[[Category: Schultz PG]]
[[Category: Stevens RC]]
[[Category: Xuan W]]