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| <StructureSection load='6b6b' size='340' side='right'caption='[[6b6b]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='6b6b' size='340' side='right'caption='[[6b6b]], [[Resolution|resolution]] 1.80Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[6b6b]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6B6B OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6B6B FirstGlance]. <br> | | <table><tr><td colspan='2'>[[6b6b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6B6B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6B6B FirstGlance]. <br> |
| </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6b5x|6b5x]]</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]] 1.8Å</td></tr> |
| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] </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=6b6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6b6b OCA], [https://pdbe.org/6b6b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6b6b RCSB], [https://www.ebi.ac.uk/pdbsum/6b6b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6b6b ProSAT]</span></td></tr> |
| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6b6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6b6b OCA], [http://pdbe.org/6b6b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6b6b RCSB], [http://www.ebi.ac.uk/pdbsum/6b6b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6b6b ProSAT]</span></td></tr> | |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
| | == Function == |
| == Publication Abstract from PubMed == | | [https://www.uniprot.org/uniprot/BLAC_MYCTU BLAC_MYCTU] |
| BACKGROUND: Ever since the first atomic structure of an enzyme was solved, the discovery of the mechanism and dynamics of reactions catalyzed by biomolecules has been the key goal for the understanding of the molecular processes that drive life on earth. Despite a large number of successful methods for trapping reaction intermediates, the direct observation of an ongoing reaction has been possible only in rare and exceptional cases. RESULTS: Here, we demonstrate a general method for capturing enzyme catalysis "in action" by mix-and-inject serial crystallography (MISC). Specifically, we follow the catalytic reaction of the Mycobacterium tuberculosis beta-lactamase with the third-generation antibiotic ceftriaxone by time-resolved serial femtosecond crystallography. The results reveal, in near atomic detail, antibiotic cleavage and inactivation from 30 ms to 2 s. CONCLUSIONS: MISC is a versatile and generally applicable method to investigate reactions of biological macromolecules, some of which are of immense biological significance and might be, in addition, important targets for structure-based drug design. With megahertz X-ray pulse rates expected at the Linac Coherent Light Source II and the European X-ray free-electron laser, multiple, finely spaced time delays can be collected rapidly, allowing a comprehensive description of biomolecular reactions in terms of structure and kinetics from the same set of X-ray data.
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| Enzyme intermediates captured "on the fly" by mix-and-inject serial crystallography.,Olmos JL Jr, Pandey S, Martin-Garcia JM, Calvey G, Katz A, Knoska J, Kupitz C, Hunter MS, Liang M, Oberthuer D, Yefanov O, Wiedorn M, Heyman M, Holl M, Pande K, Barty A, Miller MD, Stern S, Roy-Chowdhury S, Coe J, Nagaratnam N, Zook J, Verburgt J, Norwood T, Poudyal I, Xu D, Koglin J, Seaberg MH, Zhao Y, Bajt S, Grant T, Mariani V, Nelson G, Subramanian G, Bae E, Fromme R, Fung R, Schwander P, Frank M, White TA, Weierstall U, Zatsepin N, Spence J, Fromme P, Chapman HN, Pollack L, Tremblay L, Ourmazd A, Phillips GN Jr, Schmidt M BMC Biol. 2018 May 31;16(1):59. doi: 10.1186/s12915-018-0524-5. PMID:29848358<ref>PMID:29848358</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 6b6b" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]] | | *[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]] |
| == References ==
| |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Beta-lactamase]]
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| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Pandey, S]] | | [[Category: Mycobacterium tuberculosis H37Rv]] |
| [[Category: Schmidt, M]] | | [[Category: Pandey S]] |
| [[Category: Hydrolase]] | | [[Category: Schmidt M]] |