3ql0

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Current revision (10:48, 21 February 2024) (edit) (undo)
 
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<StructureSection load='3ql0' size='340' side='right'caption='[[3ql0]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='3ql0' size='340' side='right'caption='[[3ql0]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3ql0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecout Ecout]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QL0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QL0 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3ql0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_UTI89 Escherichia coli UTI89]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QL0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QL0 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=FOL:FOLIC+ACID'>FOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ql3|3ql3]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FOL:FOLIC+ACID'>FOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">folA, UTI89_C0054 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=364106 ECOUT])</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/Dihydrofolate_reductase Dihydrofolate reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.3 1.5.1.3] </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=3ql0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ql0 OCA], [https://pdbe.org/3ql0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ql0 RCSB], [https://www.ebi.ac.uk/pdbsum/3ql0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ql0 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=3ql0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ql0 OCA], [https://pdbe.org/3ql0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ql0 RCSB], [https://www.ebi.ac.uk/pdbsum/3ql0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ql0 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/Q1RGF0_ECOUT Q1RGF0_ECOUT]
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Conformational dynamics play a key role in enzyme catalysis. Although protein motions have clear implications for ligand flux, a role for dynamics in the chemical step of enzyme catalysis has not been clearly established. We generated a mutant of Escherichia coli dihydrofolate reductase that abrogates millisecond-time-scale fluctuations in the enzyme active site without perturbing its structural and electrostatic preorganization. This dynamic knockout severely impairs hydride transfer. Thus, we have found a link between conformational fluctuations on the millisecond time scale and the chemical step of an enzymatic reaction, with broad implications for our understanding of enzyme mechanisms and for design of novel protein catalysts.
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A dynamic knockout reveals that conformational fluctuations influence the chemical step of enzyme catalysis.,Bhabha G, Lee J, Ekiert DC, Gam J, Wilson IA, Dyson HJ, Benkovic SJ, Wright PE Science. 2011 Apr 8;332(6026):234-8. PMID:21474759<ref>PMID:21474759</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 3ql0" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Dihydrofolate reductase 3D structures|Dihydrofolate reductase 3D structures]]
*[[Dihydrofolate reductase 3D structures|Dihydrofolate reductase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Dihydrofolate reductase]]
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[[Category: Escherichia coli UTI89]]
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[[Category: Ecout]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Bhabha, G]]
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[[Category: Bhabha G]]
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[[Category: Ekiert, D C]]
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[[Category: Ekiert DC]]
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[[Category: Wilson, I A]]
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[[Category: Wilson IA]]
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[[Category: Wright, P E]]
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[[Category: Wright PE]]
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[[Category: Oxidoreductase]]
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[[Category: Rossmann fold]]
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Current revision

Crystal structure of N23PP/S148A mutant of E. coli dihydrofolate reductase

PDB ID 3ql0

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