1hhu
From Proteopedia
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| - | [[Image:1hhu.jpg|left|200px]]<br /><applet load="1hhu" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1hhu, resolution 0.89Å" /> | ||
| - | '''BALHIMYCIN IN COMPLEX WITH D-ALA-D-ALA'''<br /> | ||
| - | == | + | ==Balhimycin in complex with D-Ala-D-Ala== |
| + | <StructureSection load='1hhu' size='340' side='right'caption='[[1hhu]], [[Resolution|resolution]] 0.89Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1hhu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Amycolatopsis_sp. Amycolatopsis sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HHU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HHU FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.89Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3FG:(2S)-AMINO(3,5-DIHYDROXYPHENYL)ETHANOIC+ACID'>3FG</scene>, <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=DVC:(2R,4S,6S)-4-AZANYL-4,6-DIMETHYL-OXANE-2,5,5-TRIOL'>DVC</scene>, <scene name='pdbligand=GHP:(2R)-AMINO(4-HYDROXYPHENYL)ETHANOIC+ACID'>GHP</scene>, <scene name='pdbligand=MLU:N-METHYL-D-LEUCINE'>MLU</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=OMY:(BETAR)-3-CHLORO-BETA-HYDROXY-L-TYROSINE'>OMY</scene>, <scene name='pdbligand=OMZ:(BETAR)-3-CHLORO-BETA-HYDROXY-D-TYROSINE'>OMZ</scene>, <scene name='pdbligand=PRD_000484:Balhimycin'>PRD_000484</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hhu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hhu OCA], [https://pdbe.org/1hhu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hhu RCSB], [https://www.ebi.ac.uk/pdbsum/1hhu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hhu ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
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 A). 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. | 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 A). 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. | ||
| - | + | Structures of glycopeptide antibiotics with peptides that model bacterial cell-wall precursors.,Lehmann C, Bunkoczi G, Vertesy L, Sheldrick GM J Mol Biol. 2002 May 3;318(3):723-32. PMID:12054818<ref>PMID:12054818</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: Amycolatopsis sp | + | <div class="pdbe-citations 1hhu" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: Bunkoczi | + | <references/> |
| - | [[Category: Lehmann | + | __TOC__ |
| - | [[Category: Sheldrick | + | </StructureSection> |
| - | [[Category: Vertessy | + | [[Category: Amycolatopsis sp]] |
| - | + | [[Category: Large Structures]] | |
| - | + | [[Category: Bunkoczi G]] | |
| - | + | [[Category: Lehmann C]] | |
| - | + | [[Category: Sheldrick GM]] | |
| - | + | [[Category: Vertessy L]] | |
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Current revision
Balhimycin in complex with D-Ala-D-Ala
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