View source for 4mva


==1.43 Angstrom Resolution Crystal Structure of Triosephosphate Isomerase (tpiA) from Escherichia coli in Complex with Acetyl Phosphate.==
<StructureSection load='4mva' size='340' side='right'caption='[[4mva]], [[Resolution|resolution]] 1.43&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4mva]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BW2952 Escherichia coli BW2952]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MVA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MVA 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]] 1.43&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=UVW:ACETYLPHOSPHATE'>UVW</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=4mva FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mva OCA], [https://pdbe.org/4mva PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mva RCSB], [https://www.ebi.ac.uk/pdbsum/4mva PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mva ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
The emerging view of Nepsilon-lysine acetylation in eukaryotes is of a relatively abundant post-translational modification (PTM) that has a major impact on the function, structure, stability and/or location of thousands of proteins involved in diverse cellular processes. This PTM is typically considered to arise by the donation of the acetyl group from acetyl-coenzyme A (acCoA) to the epsilon-amino group of a lysine residue that is reversibly catalyzed by lysine acetyltransferases and deacetylases. Here, we provide genetic, mass spectrometric, biochemical and structural evidence that Nepsilon-lysine acetylation is an equally abundant and important PTM in bacteria. Applying a recently developed, label-free and global mass spectrometric approach to an isogenic set of mutants, we detected acetylation of thousands of lysine residues on hundreds of Escherichia coli proteins that participate in diverse and often essential cellular processes, including translation, transcription and central metabolism. Many of these acetylations were regulated in an acetyl phosphate (acP)-dependent manner, providing compelling evidence for a recently reported mechanism of bacterial Nepsilon-lysine acetylation. These mass spectrometric data, coupled with observations made by crystallography, biochemistry, and additional mass spectrometry showed that this acP-dependent acetylation is both non-enzymatic and specific, with specificity determined by the accessibility, reactivity and three-dimensional microenvironment of the target lysine. Crystallographic evidence shows acP can bind to proteins in active sites and cofactor binding sites, but also potentially anywhere molecules with a phosphate moiety could bind. Finally, we provide evidence that acP-dependent acetylation can impact the function of critical enzymes, including glyceraldehyde-3-phosphate dehydrogenase, triosephosphate isomerase, and RNA polymerase.

Structural, kinetic and proteomic characterization of acetyl phosphate-dependent bacterial protein acetylation.,Kuhn ML, Zemaitaitis B, Hu LI, Sahu A, Sorensen D, Minasov G, Lima BP, Scholle M, Mrksich M, Anderson WF, Gibson BW, Schilling B, Wolfe AJ PLoS One. 2014 Apr 22;9(4):e94816. doi: 10.1371/journal.pone.0094816. eCollection, 2014. PMID:24756028<ref>PMID:24756028</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 4mva" style="background-color:#fffaf0;"></div>

==See Also==
*[[Triose phosphate isomerase 3D structures|Triose phosphate isomerase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli BW2952]]
[[Category: Large Structures]]
[[Category: Anderson WF]]
[[Category: Dubrovska I]]
[[Category: Grimshaw S]]
[[Category: Kuhn ML]]
[[Category: Kwon K]]
[[Category: Minasov G]]
[[Category: Shuvalova L]]
[[Category: Winsor J]]