pubmed-article:8424800 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8424800 | lifeskim:mentions | umls-concept:C0029246 | lld:lifeskim |
pubmed-article:8424800 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
pubmed-article:8424800 | lifeskim:mentions | umls-concept:C1706395 | lld:lifeskim |
pubmed-article:8424800 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
pubmed-article:8424800 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
pubmed-article:8424800 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
pubmed-article:8424800 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
pubmed-article:8424800 | lifeskim:mentions | umls-concept:C0207105 | lld:lifeskim |
pubmed-article:8424800 | lifeskim:mentions | umls-concept:C1707271 | lld:lifeskim |
pubmed-article:8424800 | pubmed:dateCreated | 1993-2-23 | lld:pubmed |
pubmed-article:8424800 | pubmed:abstractText | The structural organization of penicillin-binding protein (PBP) 5 was investigated by C-terminal truncation. Compared with other low-M(r) penicillin-interacting proteins, PBP5 carries a C-terminal extension of about 100 amino acids. The sites for introduction of stop codons were chosen on the basis of the established three-dimensional structure of the Streptomyces albus G beta-lactamase [Dideberg, Charlier, Wéry, Dehottay, Dusart, Erpicum, Frère and Ghuysen (1987) Biochem. J. 245, 911-913] and comparative hydrophobic cluster analysis [Gaboriaud, Bissery, Bencheritt and Mornon (1987) FEBS Lett. 224, 149-155]. Two stop codons were introduced at positions Ile-354 or Val-348 to construct an optimized soluble form of PBP5 for crystallization purposes. The newly constructed soluble and enzymically active form (PBP5s353) was isolated by dye-affinity chromatography and gave rise to small crystals. Another two stop codons were introduced at positions Arg-261 or Ala-276 to determine the minimal enzymically active 'core protein'. The truncated form (PBP5s275), missing the entire C-terminal extension, showed unaltered penicillin-binding characteristics and a catalytic-centre activity 40% that of PBP5s353 + 9 using bisacetyl-L-Lys-D-Ala-D-Ala as substrate. This protein, however was more susceptible to proteolytic degradation, which might indicate a role of the C-terminal portion in stabilizing the protein. | lld:pubmed |
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pubmed-article:8424800 | pubmed:language | eng | lld:pubmed |
pubmed-article:8424800 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8424800 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:8424800 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8424800 | pubmed:month | Jan | lld:pubmed |
pubmed-article:8424800 | pubmed:issn | 0264-6021 | lld:pubmed |
pubmed-article:8424800 | pubmed:author | pubmed-author:van der... | lld:pubmed |
pubmed-article:8424800 | pubmed:author | pubmed-author:KeckWW | lld:pubmed |
pubmed-article:8424800 | pubmed:author | pubmed-author:de HaasCC | lld:pubmed |
pubmed-article:8424800 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8424800 | pubmed:day | 15 | lld:pubmed |
pubmed-article:8424800 | pubmed:volume | 289 ( Pt 2) | lld:pubmed |
pubmed-article:8424800 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8424800 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8424800 | pubmed:pagination | 593-8 | lld:pubmed |
pubmed-article:8424800 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:8424800 | pubmed:year | 1993 | lld:pubmed |
pubmed-article:8424800 | pubmed:articleTitle | Domain organization of penicillin-binding protein 5 from Escherichia coli analysed by C-terminal truncation. | lld:pubmed |
pubmed-article:8424800 | pubmed:affiliation | Department of Biochemistry, University of Groningen, The Netherlands. | lld:pubmed |
pubmed-article:8424800 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8424800 | pubmed:publicationType | Comparative Study | lld:pubmed |
literatureCitation:3760_842... | literatureCitation:pubmed | pubmed-article:8424800 | lld:drugbank |
entrez-gene:945222 | entrezgene:pubmed | pubmed-article:8424800 | lld:entrezgene |
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