2xr0: Difference between revisions

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[[Image:2xr0.png|left|200px]]


{{STRUCTURE_2xr0| PDB=2xr0 | SCENE= }}
==Room temperature X-ray structure of the perdeuterated Toho-1 R274N R276N double mutant beta-lactamase==
<StructureSection load='2xr0' size='340' side='right'caption='[[2xr0]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2xr0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XR0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XR0 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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2xr0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xr0 OCA], [https://pdbe.org/2xr0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xr0 RCSB], [https://www.ebi.ac.uk/pdbsum/2xr0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xr0 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BLT1_ECOLX BLT1_ECOLX] Has strong cefotaxime-hydrolyzing activity.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Room temperature neutron diffraction data of the fully perdeuterated Toho-1 R274N/R276N double mutant beta-lactamase in the apo form were used to visualize deuterium atoms within the active site of the enzyme. This perdeuterated neutron structure of the Toho-1 R274N/R276N reveals the clearest picture yet of the ground-state active site protonation states and the complete hydrogen-bonding network in a beta-lactamase enzyme. The ground-state active site protonation states detailed in this neutron diffraction study are consistent with previous high-resolution X-ray studies that support the role of Glu166 as the general base during the acylation reaction in the class A beta-lactamase reaction pathway.


===ROOM TEMPERATURE X-RAY STRUCTURE OF THE PERDEUTERATED TOHO-1 R274N R276N DOUBLE MUTANT BETA-LACTAMASE===
The active site protonation states of perdeuterated Toho-1 beta-lactamase determined by neutron diffraction support a role for Glu166 as the general base in acylation.,Tomanicek SJ, Wang KK, Weiss KL, Blakeley MP, Cooper J, Chen Y, Coates L FEBS Lett. 2010 Dec 17. PMID:21168411<ref>PMID:21168411</ref>


{{ABSTRACT_PUBMED_21168411}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
==About this Structure==
<div class="pdbe-citations 2xr0" style="background-color:#fffaf0;"></div>
[[2xr0]] is a 1 chain structure of [[Beta-lactamase]] with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XR0 OCA].


==See Also==
==See Also==
*[[Beta-lactamase|Beta-lactamase]]
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:021168411</ref><references group="xtra"/>
__TOC__
[[Category: Beta-lactamase]]
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Blakeley, M P.]]
[[Category: Large Structures]]
[[Category: Chen, Y.]]
[[Category: Blakeley MP]]
[[Category: Coates, L.]]
[[Category: Chen Y]]
[[Category: Cooper, J.]]
[[Category: Coates L]]
[[Category: Tomanicek, S J.]]
[[Category: Cooper J]]
[[Category: Wang, K K.]]
[[Category: Tomanicek SJ]]
[[Category: Weiss, K L.]]
[[Category: Wang KK]]
[[Category: Ctx-m-type esbl]]
[[Category: Weiss KL]]
[[Category: Esbl]]
[[Category: Extended-spectrum beta-lactamase]]
[[Category: Hydrolase]]