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[[ | ==Crystallographic structure of Bacillus licheniformis beta-lactamase W210F/W229F/W251F at 1.73 angstrom resolution== | ||
<StructureSection load='3soi' size='340' side='right' caption='[[3soi]], [[Resolution|resolution]] 1.73Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3soi]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SOI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SOI FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4blm|4blm]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">penP, blaP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1402 Bacillus licheniformis])</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3soi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3soi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3soi RCSB], [http://www.ebi.ac.uk/pdbsum/3soi PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
beta-lactamases confer antibiotic resistance, one of the most serious world-wide health problems, and are an excellent theoretical and experimental model in the study of protein structure, dynamics and evolution. Bacillus licheniformis exo-small penicillinase (ESP) is a Class-A beta-lactamase with three tryptophan residues located in the protein core. Here, we report the 1.7-A resolution X-ray structure, catalytic parameters, and thermodynamic stability of ESP(DeltaW), an engineered mutant of ESP in which phenylalanine replaces the wild-type tryptophan residues. The structure revealed no qualitative conformational changes compared with thirteen previously reported structures of B. licheniformis beta-lactamases (RMSD = 0.4-1.2 A). However, a closer scrutiny showed that the mutations result in an overall more compact structure, with most atoms shifted toward the geometric center of the molecule. Thus, ESP(DeltaW) has a significantly smaller radius of gyration (R(g)) than the other B. licheniformis beta-lactamases characterized so far. Indeed, ESP(DeltaW) has the smallest R(g) among 126 Class-A beta-lactamases in the Protein Data Bank (PDB). Other measures of compactness, like the number of atoms in fixed volumes and the number and average of noncovalent distances, confirmed the effect. ESP(DeltaW) proves that the compactness of the native state can be enhanced by protein engineering and establishes a new lower limit to the compactness of the Class-A beta-lactamase fold. As the condensation achieved by the native state is a paramount notion in protein folding, this result may contribute to a better understanding of how the sequence determines the conformational variability and thermodynamic stability of a given fold. | |||
X-ray evidence of a native state with increased compactness populated by tryptophan-less B. licheniformis beta-lactamase.,Risso VA, Acierno JP, Capaldi S, Monaco HL, Ermacora MR Protein Sci. 2012 Jul;21(7):964-76. doi: 10.1002/pro.2076. Epub 2012 May 31. PMID:22496053<ref>PMID:22496053</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Beta-lactamase|Beta-lactamase]] | *[[Beta-lactamase|Beta-lactamase]] | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacillus licheniformis]] | [[Category: Bacillus licheniformis]] | ||
[[Category: Beta-lactamase]] | [[Category: Beta-lactamase]] | ||
[[Category: Acierno, J P | [[Category: Acierno, J P]] | ||
[[Category: Capaldi, S | [[Category: Capaldi, S]] | ||
[[Category: Ermacora, M R | [[Category: Ermacora, M R]] | ||
[[Category: Monaco, H L | [[Category: Monaco, H L]] | ||
[[Category: Risso, V A | [[Category: Risso, V A]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
Revision as of 16:45, 9 December 2014
Crystallographic structure of Bacillus licheniformis beta-lactamase W210F/W229F/W251F at 1.73 angstrom resolutionCrystallographic structure of Bacillus licheniformis beta-lactamase W210F/W229F/W251F at 1.73 angstrom resolution
Structural highlights
Publication Abstract from PubMedbeta-lactamases confer antibiotic resistance, one of the most serious world-wide health problems, and are an excellent theoretical and experimental model in the study of protein structure, dynamics and evolution. Bacillus licheniformis exo-small penicillinase (ESP) is a Class-A beta-lactamase with three tryptophan residues located in the protein core. Here, we report the 1.7-A resolution X-ray structure, catalytic parameters, and thermodynamic stability of ESP(DeltaW), an engineered mutant of ESP in which phenylalanine replaces the wild-type tryptophan residues. The structure revealed no qualitative conformational changes compared with thirteen previously reported structures of B. licheniformis beta-lactamases (RMSD = 0.4-1.2 A). However, a closer scrutiny showed that the mutations result in an overall more compact structure, with most atoms shifted toward the geometric center of the molecule. Thus, ESP(DeltaW) has a significantly smaller radius of gyration (R(g)) than the other B. licheniformis beta-lactamases characterized so far. Indeed, ESP(DeltaW) has the smallest R(g) among 126 Class-A beta-lactamases in the Protein Data Bank (PDB). Other measures of compactness, like the number of atoms in fixed volumes and the number and average of noncovalent distances, confirmed the effect. ESP(DeltaW) proves that the compactness of the native state can be enhanced by protein engineering and establishes a new lower limit to the compactness of the Class-A beta-lactamase fold. As the condensation achieved by the native state is a paramount notion in protein folding, this result may contribute to a better understanding of how the sequence determines the conformational variability and thermodynamic stability of a given fold. X-ray evidence of a native state with increased compactness populated by tryptophan-less B. licheniformis beta-lactamase.,Risso VA, Acierno JP, Capaldi S, Monaco HL, Ermacora MR Protein Sci. 2012 Jul;21(7):964-76. doi: 10.1002/pro.2076. Epub 2012 May 31. PMID:22496053[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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