7uhq: Difference between revisions
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The | ==Time-Resolved Structure of Metallo Beta-Lactamase L1 in a Complex with Cleaved Moxalactam (4000 ms Snapshot)== | ||
<StructureSection load='7uhq' size='340' side='right'caption='[[7uhq]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7uhq]] 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=7UHQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UHQ 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]] 2.2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=XQP:(2R)-2-[(R)-carboxy{[(2R)-2-carboxy-2-(4-hydroxyphenyl)acetyl]amino}methoxymethyl]-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-oxazine-4-carboxylic+acid'>XQP</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=7uhq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7uhq OCA], [https://pdbe.org/7uhq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7uhq RCSB], [https://www.ebi.ac.uk/pdbsum/7uhq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7uhq ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/B2FTM1_STRMK B2FTM1_STRMK] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Serial 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<ref>PMID:36450742</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7uhq" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Kim | [[Category: Large Structures]] | ||
[[Category: Lavens | [[Category: Stenotrophomonas maltophilia K279a]] | ||
[[Category: | [[Category: Babnigg G]] | ||
[[Category: | [[Category: Endres M]] | ||
[[Category: | [[Category: Henning R]] | ||
[[Category: | [[Category: Joachimiak A]] | ||
[[Category: Kim Y]] | |||
[[Category: Lavens A]] | |||
[[Category: Maltseva N]] | |||
[[Category: Sherrell DA]] | |||
[[Category: Srajer V]] | |||
[[Category: Wilamowski M]] | |||
Latest revision as of 12:53, 25 October 2023
Time-Resolved Structure of Metallo Beta-Lactamase L1 in a Complex with Cleaved Moxalactam (4000 ms Snapshot)Time-Resolved Structure of Metallo Beta-Lactamase L1 in a Complex with Cleaved Moxalactam (4000 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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