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7lxg

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<StructureSection load='7lxg' size='340' side='right'caption='[[7lxg]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='7lxg' size='340' side='right'caption='[[7lxg]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7lxg]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LXG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LXG FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7lxg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LXG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LXG FirstGlance]. <br>
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</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=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</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=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=YHA:Homocitrulline'>YHA</scene></td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=YHA:'>YHA</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7lxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lxg OCA], [https://pdbe.org/7lxg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lxg RCSB], [https://www.ebi.ac.uk/pdbsum/7lxg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lxg ProSAT]</span></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=7lxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lxg OCA], [https://pdbe.org/7lxg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lxg RCSB], [https://www.ebi.ac.uk/pdbsum/7lxg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lxg ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[[https://www.uniprot.org/uniprot/Q6XEC0_KLEPN Q6XEC0_KLEPN]]
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Carbon dioxide is an omnipresent gas that drives adaptive responses within organisms from all domains of life. The molecular mechanisms by which proteins serve as sensors of CO2 are, accordingly, of great interest. Because CO2 is electrophilic, one way it can modulate protein biochemistry is by carboxylation of the amine group of lysine residues. However, the resulting CO2-carboxylated lysines spontaneously decompose, giving off CO2, which makes studying this modification difficult. Here we describe a method to stably mimic CO2-carboxylated lysine residues in proteins. We leverage this method to develop a quantitative approach to identify CO2-carboxylated lysines of proteins and explore the lysine 'carboxylome' of the CO2-responsive cyanobacterium Synechocystis sp. We uncover one CO2-carboxylated lysine within the effector binding pocket of the metabolic signaling protein PII. CO2-carboxylatation of this lysine markedly lowers the affinity of PII for its regulatory effector ligand ATP, illuminating a negative molecular control mechanism mediated by CO2.
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Chemoproteomic identification of CO2-dependent lysine carboxylation in proteins.,King DT, Zhu S, Hardie DB, Serrano-Negron JE, Madden Z, Kolappan S, Vocadlo DJ Nat Chem Biol. 2022 Jul;18(7):782-791. doi: 10.1038/s41589-022-01043-1. Epub 2022, Jun 16. PMID:35710617<ref>PMID:35710617</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 7lxg" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Beta-lactamase]]
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[[Category: Klebsiella pneumoniae]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: King, D T]]
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[[Category: King DT]]
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[[Category: Serrano-Negron, J E]]
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[[Category: Serrano-Negron JE]]
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[[Category: Vocadlo, D J]]
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[[Category: Vocadlo DJ]]
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[[Category: Homocitrulline]]
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[[Category: Hydrolase]]
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[[Category: Oxa-48]]
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Revision as of 06:23, 8 September 2022

Homocitrullinated beta-lactamase OXA-48

PDB ID 7lxg

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