The structure of Toho1 β‐lactamase in complex with penicillin reveals the role of Tyr105 in substrate recognition
The role of the conserved residue Tyr105 in class A β‐lactamases has been the subject of investigation using both structural studies and saturation mutagenesis. Both have shown that while it does not need to be strictly conserved for activity, it is important for substrate recognition. With this in...
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| Published in | FEBS open bio Vol. 6; no. 12; pp. 1170 - 1177 |
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| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
England
John Wiley & Sons, Inc
01.12.2016
Wiley Blackwell (John Wiley & Sons) John Wiley and Sons Inc Wiley |
| Subjects | |
| Online Access | Get full text |
| ISSN | 2211-5463 2211-5463 |
| DOI | 10.1002/2211-5463.12132 |
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| Abstract | The role of the conserved residue Tyr105 in class A β‐lactamases has been the subject of investigation using both structural studies and saturation mutagenesis. Both have shown that while it does not need to be strictly conserved for activity, it is important for substrate recognition. With this in mind we determined the crystal structure of Toho1 β‐lactamase at 15 K to 1.10 Å resolution in complex with penicillin. As expected a ring‐opened penicillin molecule bound to Ser70 the catalytic nucleophile, can clearly be seen in electron density in the active site. In addition to the trapped penicillin, however, are two additional intact ring‐closed penicillin molecules, captured by the enzyme through noncovalent interactions at the edge of the active site.
To investigate the role of the conserved residue Tyr105 in class A β‐lactamases, the crystal structure of Toho1 β‐lactamase complexed with penicillin was solved at 15 K to 1.10 Å resolution. Visualization of the complex reveals the interactions necessary for substrate recognition and binding, and provides insight into how these interactions may drive enzyme function. |
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| AbstractList | The role of the conserved residue Tyr105 in class A β-lactamases has been the subject of investigation using both structural studies and saturation mutagenesis. Both have shown that while it does not need to be strictly conserved for activity, it is important for substrate recognition. With this in mind we determined the crystal structure of Toho1 β-lactamase at 15 K to 1.10 Å resolution in complex with penicillin. As expected a ring-opened penicillin molecule bound to Ser70 the catalytic nucleophile, can clearly be seen in electron density in the active site. In addition to the trapped penicillin, however, are two additional intact ring-closed penicillin molecules, captured by the enzyme through noncovalent interactions at the edge of the active site.The role of the conserved residue Tyr105 in class A β-lactamases has been the subject of investigation using both structural studies and saturation mutagenesis. Both have shown that while it does not need to be strictly conserved for activity, it is important for substrate recognition. With this in mind we determined the crystal structure of Toho1 β-lactamase at 15 K to 1.10 Å resolution in complex with penicillin. As expected a ring-opened penicillin molecule bound to Ser70 the catalytic nucleophile, can clearly be seen in electron density in the active site. In addition to the trapped penicillin, however, are two additional intact ring-closed penicillin molecules, captured by the enzyme through noncovalent interactions at the edge of the active site. The role of the conserved residue Tyr105 in class A β‐lactamases has been the subject of investigation using both structural studies and saturation mutagenesis. Both have shown that while it does not need to be strictly conserved for activity, it is important for substrate recognition. With this in mind we determined the crystal structure of Toho1 β‐lactamase at 15 K to 1.10 Å resolution in complex with penicillin. As expected a ring‐opened penicillin molecule bound to Ser70 the catalytic nucleophile, can clearly be seen in electron density in the active site. In addition to the trapped penicillin, however, are two additional intact ring‐closed penicillin molecules, captured by the enzyme through noncovalent interactions at the edge of the active site. The role of the conserved residue Tyr105 in class A β‐lactamases has been the subject of investigation using both structural studies and saturation mutagenesis. Both have shown that while it does not need to be strictly conserved for activity, it is important for substrate recognition. With this in mind we determined the crystal structure of Toho1 β‐lactamase at 15 K to 1.10 Å resolution in complex with penicillin. As expected a ring‐opened penicillin molecule bound to Ser70 the catalytic nucleophile, can clearly be seen in electron density in the active site. In addition to the trapped penicillin, however, are two additional intact ring‐closed penicillin molecules, captured by the enzyme through noncovalent interactions at the edge of the active site. To investigate the role of the conserved residue Tyr105 in class A β‐lactamases, the crystal structure of Toho1 β‐lactamase complexed with penicillin was solved at 15 K to 1.10 Å resolution. Visualization of the complex reveals the interactions necessary for substrate recognition and binding, and provides insight into how these interactions may drive enzyme function. |
| Author | Vandavasi, Venu Gopal Weiss, Kevin L. Langan, Patricia S. Coates, Leighton Cooper, Jonathan B. Ginell, Stephan L. |
| AuthorAffiliation | 2 Birkbeck University of London UK 3 Structural Biology Center Argonne National Laboratory IL USA 1 Biology and Soft Matter Division Oak Ridge National Laboratory TN USA |
| AuthorAffiliation_xml | – name: 3 Structural Biology Center Argonne National Laboratory IL USA – name: 1 Biology and Soft Matter Division Oak Ridge National Laboratory TN USA – name: 2 Birkbeck University of London UK |
| Author_xml | – sequence: 1 givenname: Patricia S. surname: Langan fullname: Langan, Patricia S. organization: Oak Ridge National Laboratory – sequence: 2 givenname: Venu Gopal surname: Vandavasi fullname: Vandavasi, Venu Gopal organization: Oak Ridge National Laboratory – sequence: 3 givenname: Kevin L. surname: Weiss fullname: Weiss, Kevin L. organization: Oak Ridge National Laboratory – sequence: 4 givenname: Jonathan B. surname: Cooper fullname: Cooper, Jonathan B. organization: Birkbeck University of London – sequence: 5 givenname: Stephan L. surname: Ginell fullname: Ginell, Stephan L. organization: Argonne National Laboratory – sequence: 6 givenname: Leighton surname: Coates fullname: Coates, Leighton email: coatesl@ornl.gov organization: Oak Ridge National Laboratory |
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| CitedBy_id | crossref_primary_10_1007_s10858_021_00375_9 crossref_primary_10_1021_acscatal_7b04114 crossref_primary_10_1073_pnas_1922203117 crossref_primary_10_1021_acsphyschemau_2c00005 crossref_primary_10_1039_D1OB01593A crossref_primary_10_1128_AAC_00398_20 crossref_primary_10_1142_S2737416523500217 crossref_primary_10_7554_eLife_83928 crossref_primary_10_1073_pnas_1819859116 crossref_primary_10_1016_j_retram_2019_05_003 |
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| Keywords | enzyme antibiotic resistance antibiotics X‐ray crystallography enzyme structure |
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| Snippet | The role of the conserved residue Tyr105 in class A β‐lactamases has been the subject of investigation using both structural studies and saturation... The role of the conserved residue Tyr105 in class A β-lactamases has been the subject of investigation using both structural studies and saturation... |
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| SubjectTerms | Amino acids antibiotic resistance Antibiotics Bacteria Biochemistry & Molecular Biology Construction contracts Crystal structure Energy Environmental research enzyme enzyme structure Enzymes Hydrogen bonds Laboratories Penicillin Proteins R&D Research & development Saturation mutagenesis X-ray crystallograph X‐ray crystallography |
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| Title | The structure of Toho1 β‐lactamase in complex with penicillin reveals the role of Tyr105 in substrate recognition |
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