Structures of Glycopeptide Antibiotics with Peptides that Model Bacterial Cell-Wall Precursors
The vancomycin-related antibiotics balhimycin and degluco-balhimycin have been crystallized in complexes with di-, tri- and pentapeptides that emulate bacterial cell-wall precursors, and four structures determined at atomic resolution (
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| Veröffentlicht in: | Journal of molecular biology 2002-05, Vol.318 (3), p.723-732 |
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| container_title | Journal of molecular biology |
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| creator | Lehmann, Christopher Bunkóczi, Gábor Vértesy, László Sheldrick, George M. |
| description | The vancomycin-related antibiotics balhimycin and degluco-balhimycin have been crystallized in complexes with di-, tri- and pentapeptides that emulate bacterial cell-wall precursors, and four structures determined at atomic resolution ( |
| doi_str_mv | 10.1016/S0022-2836(02)00146-8 |
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Å). In addition to the features expected from previous structural and spectroscopic studies, two new motifs were observed that may prove important in the design of antibiotics modified to overcome bacterial resistance. A changed binding mode was found in two dipeptide complexes, and a new type of face-to-face oligomerization (in addition to the well-established back-to-back dimerization) was seen when the model peptide reaches a critical fraction of the size of the cell-wall precursor pentapeptide. The extensive interactions involving both antibiotic and peptide molecules in this interface should appreciably enhance the kinetic and thermodynamic stability of the complexes.
In the pentapeptide complex, the relative positions of the peptides are close to those required for
d-Ala elimination, so this structure may provide a realistic model for the prevention of the enzyme-catalyzed cell-wall crosslinking by antibiotic binding.</description><identifier>ISSN: 0022-2836</identifier><identifier>EISSN: 1089-8638</identifier><identifier>DOI: 10.1016/S0022-2836(02)00146-8</identifier><identifier>PMID: 12054818</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Anti-Bacterial Agents - chemistry ; bacterial cell-wall ; Bacterial Proteins - chemistry ; Binding Sites ; Cell Wall - chemistry ; crystal structure ; Crystallography, X-Ray ; Dimerization ; Drug Resistance, Bacterial ; glycopeptide antibiotics ; Ligands ; Models, Molecular ; Molecular Structure ; peptide complexes ; Protein Conformation ; Protein Precursors - chemistry ; vancomycin ; Vancomycin - analogs & derivatives ; Vancomycin - chemistry</subject><ispartof>Journal of molecular biology, 2002-05, Vol.318 (3), p.723-732</ispartof><rights>2002 Elsevier Science Ltd</rights><rights>(c) 2002 Elsevier Science Ltd.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c392t-e882ddd0997890074c5f92a8784ef0d587e17eef38fa1a71bf0b5f17064a7f343</citedby><cites>FETCH-LOGICAL-c392t-e882ddd0997890074c5f92a8784ef0d587e17eef38fa1a71bf0b5f17064a7f343</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0022283602001468$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12054818$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lehmann, Christopher</creatorcontrib><creatorcontrib>Bunkóczi, Gábor</creatorcontrib><creatorcontrib>Vértesy, László</creatorcontrib><creatorcontrib>Sheldrick, George M.</creatorcontrib><title>Structures of Glycopeptide Antibiotics with Peptides that Model Bacterial Cell-Wall Precursors</title><title>Journal of molecular biology</title><addtitle>J Mol Biol</addtitle><description>The vancomycin-related antibiotics balhimycin and degluco-balhimycin have been crystallized in complexes with di-, tri- and pentapeptides that emulate bacterial cell-wall precursors, and four structures determined at atomic resolution (<1
Å). In addition to the features expected from previous structural and spectroscopic studies, two new motifs were observed that may prove important in the design of antibiotics modified to overcome bacterial resistance. A changed binding mode was found in two dipeptide complexes, and a new type of face-to-face oligomerization (in addition to the well-established back-to-back dimerization) was seen when the model peptide reaches a critical fraction of the size of the cell-wall precursor pentapeptide. The extensive interactions involving both antibiotic and peptide molecules in this interface should appreciably enhance the kinetic and thermodynamic stability of the complexes.
In the pentapeptide complex, the relative positions of the peptides are close to those required for
d-Ala elimination, so this structure may provide a realistic model for the prevention of the enzyme-catalyzed cell-wall crosslinking by antibiotic binding.</description><subject>Anti-Bacterial Agents - chemistry</subject><subject>bacterial cell-wall</subject><subject>Bacterial Proteins - chemistry</subject><subject>Binding Sites</subject><subject>Cell Wall - chemistry</subject><subject>crystal structure</subject><subject>Crystallography, X-Ray</subject><subject>Dimerization</subject><subject>Drug Resistance, Bacterial</subject><subject>glycopeptide antibiotics</subject><subject>Ligands</subject><subject>Models, Molecular</subject><subject>Molecular Structure</subject><subject>peptide complexes</subject><subject>Protein Conformation</subject><subject>Protein Precursors - chemistry</subject><subject>vancomycin</subject><subject>Vancomycin - analogs & derivatives</subject><subject>Vancomycin - chemistry</subject><issn>0022-2836</issn><issn>1089-8638</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkcFuEzEQhi1ERUPhEUA-IThsGXu969kTKhGUSkVUKogblmOPVaNNnNpeqr49myaCY09z8Df-R9_P2CsBpwJE__4aQMpGYtu_BfkOQKi-wSdsIQCHBvsWn7LFP-SYPS_lNwB0rcJn7FhI6BQKXLBf1zVPrk6ZCk-Bn4_3Lm1pW6MnfrapcRVTja7wu1hv-NX-ofB6Yyv_mjyN_KN1lXK0I1_SODY_7Tjyq0xuyiXl8oIdBTsWenmYJ-zH50_fl1-ay2_nF8uzy8a1g6wNIUrvPQyDxgFAK9eFQVrUqCiA71CT0EShxWCF1WIVYNUFoaFXVodWtSfszf7fbU63E5Vq1rG4-SC7oTQVowXOhmYVj4ECFQip9Ax2e9DlVEqmYLY5rm2-NwLMrgHz0IDZ6TUgzUMDZhfw-hAwrdbk_28dlM_Ahz1As48_kbIpLtLGkY-ztmp8io9E_AUITpXR</recordid><startdate>20020503</startdate><enddate>20020503</enddate><creator>Lehmann, Christopher</creator><creator>Bunkóczi, Gábor</creator><creator>Vértesy, László</creator><creator>Sheldrick, George M.</creator><general>Elsevier Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>20020503</creationdate><title>Structures of Glycopeptide Antibiotics with Peptides that Model Bacterial Cell-Wall Precursors</title><author>Lehmann, Christopher ; Bunkóczi, Gábor ; Vértesy, László ; Sheldrick, George M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c392t-e882ddd0997890074c5f92a8784ef0d587e17eef38fa1a71bf0b5f17064a7f343</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Anti-Bacterial Agents - chemistry</topic><topic>bacterial cell-wall</topic><topic>Bacterial Proteins - chemistry</topic><topic>Binding Sites</topic><topic>Cell Wall - chemistry</topic><topic>crystal structure</topic><topic>Crystallography, X-Ray</topic><topic>Dimerization</topic><topic>Drug Resistance, Bacterial</topic><topic>glycopeptide antibiotics</topic><topic>Ligands</topic><topic>Models, Molecular</topic><topic>Molecular Structure</topic><topic>peptide complexes</topic><topic>Protein Conformation</topic><topic>Protein Precursors - chemistry</topic><topic>vancomycin</topic><topic>Vancomycin - analogs & derivatives</topic><topic>Vancomycin - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lehmann, Christopher</creatorcontrib><creatorcontrib>Bunkóczi, Gábor</creatorcontrib><creatorcontrib>Vértesy, László</creatorcontrib><creatorcontrib>Sheldrick, George M.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lehmann, Christopher</au><au>Bunkóczi, Gábor</au><au>Vértesy, László</au><au>Sheldrick, George M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structures of Glycopeptide Antibiotics with Peptides that Model Bacterial Cell-Wall Precursors</atitle><jtitle>Journal of molecular biology</jtitle><addtitle>J Mol Biol</addtitle><date>2002-05-03</date><risdate>2002</risdate><volume>318</volume><issue>3</issue><spage>723</spage><epage>732</epage><pages>723-732</pages><issn>0022-2836</issn><eissn>1089-8638</eissn><abstract>The vancomycin-related antibiotics balhimycin and degluco-balhimycin have been crystallized in complexes with di-, tri- and pentapeptides that emulate bacterial cell-wall precursors, and four structures determined at atomic resolution (<1
Å). In addition to the features expected from previous structural and spectroscopic studies, two new motifs were observed that may prove important in the design of antibiotics modified to overcome bacterial resistance. A changed binding mode was found in two dipeptide complexes, and a new type of face-to-face oligomerization (in addition to the well-established back-to-back dimerization) was seen when the model peptide reaches a critical fraction of the size of the cell-wall precursor pentapeptide. The extensive interactions involving both antibiotic and peptide molecules in this interface should appreciably enhance the kinetic and thermodynamic stability of the complexes.
In the pentapeptide complex, the relative positions of the peptides are close to those required for
d-Ala elimination, so this structure may provide a realistic model for the prevention of the enzyme-catalyzed cell-wall crosslinking by antibiotic binding.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>12054818</pmid><doi>10.1016/S0022-2836(02)00146-8</doi><tpages>10</tpages></addata></record> |
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| ispartof | Journal of molecular biology, 2002-05, Vol.318 (3), p.723-732 |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Anti-Bacterial Agents - chemistry bacterial cell-wall Bacterial Proteins - chemistry Binding Sites Cell Wall - chemistry crystal structure Crystallography, X-Ray Dimerization Drug Resistance, Bacterial glycopeptide antibiotics Ligands Models, Molecular Molecular Structure peptide complexes Protein Conformation Protein Precursors - chemistry vancomycin Vancomycin - analogs & derivatives Vancomycin - chemistry |
| title | Structures of Glycopeptide Antibiotics with Peptides that Model Bacterial Cell-Wall Precursors |
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