7uhh: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7uhh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Stenotrophomonas_maltophilia_K279a Stenotrophomonas maltophilia K279a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7UHH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UHH FirstGlance]. <br> | <table><tr><td colspan='2'>[[7uhh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Stenotrophomonas_maltophilia_K279a Stenotrophomonas maltophilia K279a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7UHH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UHH FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MX0:(1R,6R,7R)-7-[(2R)-2-carboxypropanamido]-7-methoxy-3-methyl-8-oxo-5-oxa-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic+acid'>MX0</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MX0:(1R,6R,7R)-7-[(2R)-2-carboxypropanamido]-7-methoxy-3-methyl-8-oxo-5-oxa-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic+acid'>MX0</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=7uhh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7uhh OCA], [https://pdbe.org/7uhh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7uhh RCSB], [https://www.ebi.ac.uk/pdbsum/7uhh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7uhh 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=7uhh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7uhh OCA], [https://pdbe.org/7uhh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7uhh RCSB], [https://www.ebi.ac.uk/pdbsum/7uhh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7uhh ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 12:52, 25 October 2023
Time-Resolved Structure of Metallo Beta-Lactamase L1 in a Complex with Non-Hydrolyzed Moxalactam (20 ms snapshot)Time-Resolved Structure of Metallo Beta-Lactamase L1 in a Complex with Non-Hydrolyzed Moxalactam (20 ms snapshot)
Structural highlights
FunctionPublication Abstract from PubMedSerial x-ray crystallography can uncover binding events, and subsequent chemical conversions occurring during enzymatic reaction. Here, we reveal the structure, binding and cleavage of moxalactam antibiotic bound to L1 metallo-beta-lactamase (MBL) from Stenotrophomonas maltophilia. Using time-resolved serial synchrotron crystallography, we show the time course of beta-lactam hydrolysis and determine ten snapshots (20, 40, 60, 80, 100, 150, 300, 500, 2000 and 4000 ms) at 2.20 A resolution. The reaction is initiated by laser pulse releasing Zn(2+) ions from a UV-labile photocage. Two metal ions bind to the active site, followed by binding of moxalactam and the intact beta-lactam ring is observed for 100 ms after photolysis. Cleavage of beta-lactam is detected at 150 ms and the ligand is significantly displaced. The reaction product adjusts its conformation reaching steady state at 2000 ms corresponding to the relaxed state of the enzyme. Only small changes are observed in the positions of Zn(2+) ions and the active site residues. Mechanistic details captured here can be generalized to other MBLs. Time-resolved beta-lactam cleavage by L1 metallo-beta-lactamase.,Wilamowski M, Sherrell DA, Kim Y, Lavens A, Henning RW, Lazarski K, Shigemoto A, Endres M, Maltseva N, Babnigg G, Burdette SC, Srajer V, Joachimiak A Nat Commun. 2022 Nov 30;13(1):7379. doi: 10.1038/s41467-022-35029-3. PMID:36450742[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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