7a5u: Difference between revisions
New page: '''Unreleased structure''' The entry 7a5u is ON HOLD Authors: Description: Category: Unreleased Structures |
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==Structure of E37A BlaC from Mycobacterium tuberculosis== | |||
<StructureSection load='7a5u' size='340' side='right'caption='[[7a5u]], [[Resolution|resolution]] 1.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7a5u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7A5U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7A5U 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]] 1.5Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</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=7a5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7a5u OCA], [https://pdbe.org/7a5u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7a5u RCSB], [https://www.ebi.ac.uk/pdbsum/7a5u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7a5u ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/BLAC_MYCTU BLAC_MYCTU] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Evolutionary robustness requires that the number of highly conserved amino acid residues in proteins is minimized. In enzymes, such conservation is observed for catalytic residues but also for some residues in the second shell or even further from the active site. beta-lactamases evolve in response to changing antibiotic selection pressures and are thus expected to be evolutionarily robust, with a limited number of highly conserved amino acid residues. As part of the effort to understand the roles of conserved residues in class A beta-lactamases, we investigate the reasons leading to the conservation of two amino acid residues in the beta-lactamase BlaC, Glu37 and Trp229. Using site-directed mutagenesis, we have generated point mutations of these residues and observed a drastic decrease in the levels of soluble protein produced in Escherichia coli, thus abolishing completely the resistance of bacteria against beta-lactam antibiotics. However, the purified proteins are structurally and kinetically very similar to the wild type enzyme, only differing by exhibiting a slightly lower melting temperature. We conclude that conservation of Glu37 and Trp229 is solely caused by an essential role in the folding process and we propose that during folding Glu37 primes the formation of the central beta-sheet and Trp229 contributes to the hydrophobic collapse into a molten globule. | |||
Conserved residues Glu37 and Trp229 play an essential role in protein folding of beta-lactamase.,Chikunova A, Manley MP, Ud Din Ahmad M, Bilman T, Perrakis A, Ubbink M FEBS J. 2021 Mar 31. doi: 10.1111/febs.15854. PMID:33792206<ref>PMID:33792206</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7a5u" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mycobacterium tuberculosis]] | |||
[[Category: Ahmad MU]] | |||
[[Category: Chikunova A]] | |||
[[Category: Perrakis A]] | |||
[[Category: Ubbink M]] | |||
Latest revision as of 15:04, 1 February 2024
Structure of E37A BlaC from Mycobacterium tuberculosisStructure of E37A BlaC from Mycobacterium tuberculosis
Structural highlights
FunctionPublication Abstract from PubMedEvolutionary robustness requires that the number of highly conserved amino acid residues in proteins is minimized. In enzymes, such conservation is observed for catalytic residues but also for some residues in the second shell or even further from the active site. beta-lactamases evolve in response to changing antibiotic selection pressures and are thus expected to be evolutionarily robust, with a limited number of highly conserved amino acid residues. As part of the effort to understand the roles of conserved residues in class A beta-lactamases, we investigate the reasons leading to the conservation of two amino acid residues in the beta-lactamase BlaC, Glu37 and Trp229. Using site-directed mutagenesis, we have generated point mutations of these residues and observed a drastic decrease in the levels of soluble protein produced in Escherichia coli, thus abolishing completely the resistance of bacteria against beta-lactam antibiotics. However, the purified proteins are structurally and kinetically very similar to the wild type enzyme, only differing by exhibiting a slightly lower melting temperature. We conclude that conservation of Glu37 and Trp229 is solely caused by an essential role in the folding process and we propose that during folding Glu37 primes the formation of the central beta-sheet and Trp229 contributes to the hydrophobic collapse into a molten globule. Conserved residues Glu37 and Trp229 play an essential role in protein folding of beta-lactamase.,Chikunova A, Manley MP, Ud Din Ahmad M, Bilman T, Perrakis A, Ubbink M FEBS J. 2021 Mar 31. doi: 10.1111/febs.15854. PMID:33792206[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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