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Structure paper

TitleEvolution of an antibiotic resistance enzyme constrained by stability and activity trade-offs.
Journal, issue, pagesJ. Mol. Biol., Vol. 320, Page 85-95, Year 2002
Publish dateSep 4, 2001 (structure data deposition date)
AuthorsWang, X. / Minasov, G. / Shoichet, B.K.
External linksJ. Mol. Biol. / PubMed:12079336
MethodsX-ray diffraction
Resolution1.75 - 1.85 Å
Structure data

PDB-1jwp:
Structure of M182T mutant of TEM-1 beta-lactamase
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

PDB-1jwv:
Crystal structure of G238A mutant of TEM-1 beta-lactamase in complex with a boronic acid inhibitor (sefb4)
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-1jwz:
Crystal structure of TEM-64 beta-lactamase in complex with a boronic acid inhibitor (105)
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION

ChemComp-HOH:
WATER

ChemComp-K:
Unknown entry

ChemComp-CB4:
PINACOL[[2-AMINO-ALPHA-(1-CARBOXY-1-METHYLETHOXYIMINO)-4-THIAZOLEACETYL]AMINO]METHANEBORONATE

ChemComp-105:
N-[5-METHYL-3-O-TOLYL-ISOXAZOLE-4-CARBOXYLIC ACID AMIDE] BORONIC ACID

Source
  • escherichia coli (E. coli)
KeywordsHYDROLASE / Protein stability / TEM-1 / beta-lactamase / antibiotic resistance / evolution / serine hydrolase / tem-64

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