Entry | Database: PDB / ID: 6vbd |
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Title | Crystal structure of transpeptidase domain of PBP2 from Neisseria gonorrhoeae cephalosporin-resistant strain H041 acylated by ceftriaxone |
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Components | Probable peptidoglycan D,D-transpeptidase PenA |
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Keywords | HYDROLASE/ANTIBIOTIC / PENICILLIN-BINDING PROTEIN / ACYLATION / ANTIBIOTIC RESISTANCE / HYDROLASE / HYDROLASE-ANTIBIOTIC complex |
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Function / homology | Function and homology information
peptidoglycan glycosyltransferase activity / serine-type D-Ala-D-Ala carboxypeptidase / FtsZ-dependent cytokinesis / serine-type D-Ala-D-Ala carboxypeptidase activity / division septum assembly / penicillin binding / peptidoglycan biosynthetic process / cell wall organization / regulation of cell shape / response to antibiotic ...peptidoglycan glycosyltransferase activity / serine-type D-Ala-D-Ala carboxypeptidase / FtsZ-dependent cytokinesis / serine-type D-Ala-D-Ala carboxypeptidase activity / division septum assembly / penicillin binding / peptidoglycan biosynthetic process / cell wall organization / regulation of cell shape / response to antibiotic / proteolysis / plasma membraneSimilarity search - Function Peptidoglycan D,D-transpeptidase FtsI / Penicillin-binding protein, dimerisation domain / Penicillin-binding Protein dimerisation domain / Penicillin-binding protein, dimerisation domain superfamily / : / Penicillin-binding protein, transpeptidase / Penicillin binding protein transpeptidase domain / Beta-lactamase / DD-peptidase/beta-lactamase superfamily / Beta-lactamase/transpeptidase-like ...Peptidoglycan D,D-transpeptidase FtsI / Penicillin-binding protein, dimerisation domain / Penicillin-binding Protein dimerisation domain / Penicillin-binding protein, dimerisation domain superfamily / : / Penicillin-binding protein, transpeptidase / Penicillin binding protein transpeptidase domain / Beta-lactamase / DD-peptidase/beta-lactamase superfamily / Beta-lactamase/transpeptidase-like / 3-Layer(aba) Sandwich / Alpha BetaSimilarity search - Domain/homology |
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Biological species | Neisseria gonorrhoeae (bacteria) |
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Method | X-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 1.8 Å |
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Authors | Singh, A. / Davies, C. |
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Funding support | United States, 1items Organization | Grant number | Country |
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National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) | GM066861 | United States |
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Citation | Journal: J.Biol.Chem. / Year: 2020 Title: Mutations in Neisseria gonorrhoeae penicillin-binding protein 2 associated with extended-spectrum cephalosporin resistance create an energetic barrier against acylation via restriction of protein dynamics Authors: Singh, A. / Turner, J. / Tomberg, J. / Fedarovich, A. / Unemo, M. / Nicholas, R.A. / Davies, C. |
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History | Deposition | Dec 18, 2019 | Deposition site: RCSB / Processing site: RCSB |
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Revision 1.0 | Apr 15, 2020 | Provider: repository / Type: Initial release |
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