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[[Image:1c0q.gif|left|200px]]


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==COMPLEX OF VANCOMYCIN WITH 2-ACETOXY-D-PROPANOIC ACID==
The line below this paragraph, containing "STRUCTURE_1c0q", creates the "Structure Box" on the page.
<StructureSection load='1c0q' size='340' side='right'caption='[[1c0q]], [[Resolution|resolution]] 1.00&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1c0q]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Amycolatopsis_orientalis Amycolatopsis orientalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C0Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C0Q FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1&#8491;</td></tr>
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<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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GHP:(2R)-AMINO(4-HYDROXYPHENYL)ETHANOIC+ACID'>GHP</scene>, <scene name='pdbligand=LAC:LACTIC+ACID'>LAC</scene>, <scene name='pdbligand=MLU:N-METHYL-D-LEUCINE'>MLU</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_000204:Vancomycin'>PRD_000204</scene>, <scene name='pdbligand=RER:(1R,3S,4S,5S)-3-AMINO-2,3,6-TRIDEOXY-3-METHYL-ALPHA-L-ARABINO-HEXOPYRANOSE'>RER</scene></td></tr>
{{STRUCTURE_1c0q|  PDB=1c0q  |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1c0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c0q OCA], [https://pdbe.org/1c0q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c0q RCSB], [https://www.ebi.ac.uk/pdbsum/1c0q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c0q ProSAT]</span></td></tr>
 
</table>
'''COMPLEX OF VANCOMYCIN WITH 2-ACETOXY-D-PROPANOIC ACID'''
<div style="background-color:#fffaf0;">
 
== Publication Abstract from PubMed ==
 
==Overview==
Bacterial resistance to vancomycin has been attributed to the loss of an intermolecular hydrogen bond between vancomycin and its peptidoglycan target when cell wall biosynthesis proceeds via depsipeptide intermediates rather than the usual polypeptide intermediates. To investigate the relative importance of this hydrogen bond to vancomycin binding, we have determined crystal structures at 1.0 A resolution for the vancomycin complexes with three ligands that mimic peptides and depsipeptides found in vancomycin-sensitive and vancomycin-resistant bacteria: N-acetylglycine, D-lactic acid, and 2-acetoxy-D-propanoic acid. These, in conjunction with structures that have been reported previously, indicate higher-affinity ligands elicit a structural change in the drug not seen with these low-affinity ligands. They also enable us to define a minimal set of drug-ligand interactions necessary to confer higher-affinity binding on a ligand. Most importantly, these structures point to factors in addition to the loss of an intermolecular hydrogen bond that must be invoked to explain the weaker affinity of vancomycin for depsipeptide ligands. These factors are important considerations for the design of vancomycin analogues to overcome vancomycin resistance.
Bacterial resistance to vancomycin has been attributed to the loss of an intermolecular hydrogen bond between vancomycin and its peptidoglycan target when cell wall biosynthesis proceeds via depsipeptide intermediates rather than the usual polypeptide intermediates. To investigate the relative importance of this hydrogen bond to vancomycin binding, we have determined crystal structures at 1.0 A resolution for the vancomycin complexes with three ligands that mimic peptides and depsipeptides found in vancomycin-sensitive and vancomycin-resistant bacteria: N-acetylglycine, D-lactic acid, and 2-acetoxy-D-propanoic acid. These, in conjunction with structures that have been reported previously, indicate higher-affinity ligands elicit a structural change in the drug not seen with these low-affinity ligands. They also enable us to define a minimal set of drug-ligand interactions necessary to confer higher-affinity binding on a ligand. Most importantly, these structures point to factors in addition to the loss of an intermolecular hydrogen bond that must be invoked to explain the weaker affinity of vancomycin for depsipeptide ligands. These factors are important considerations for the design of vancomycin analogues to overcome vancomycin resistance.


==About this Structure==
Vancomycin binding to low-affinity ligands: delineating a minimum set of interactions necessary for high-affinity binding.,Loll PJ, Kaplan J, Selinsky BS, Axelsen PH J Med Chem. 1999 Nov 4;42(22):4714-9. PMID:10579833<ref>PMID:10579833</ref>
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C0Q OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Vancomycin binding to low-affinity ligands: delineating a minimum set of interactions necessary for high-affinity binding., Loll PJ, Kaplan J, Selinsky BS, Axelsen PH, J Med Chem. 1999 Nov 4;42(22):4714-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10579833 10579833]
</div>
[[Category: Axelsen, P H.]]
<div class="pdbe-citations 1c0q" style="background-color:#fffaf0;"></div>
[[Category: Kaplan, J.]]
== References ==
[[Category: Loll, P J.]]
<references/>
[[Category: Selinsky, B.]]
__TOC__
[[Category: Glycopeptide antibiotic]]
</StructureSection>
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:11:44 2008''
[[Category: Amycolatopsis orientalis]]
[[Category: Large Structures]]
[[Category: Axelsen PH]]
[[Category: Kaplan J]]
[[Category: Loll PJ]]
[[Category: Selinsky B]]

Latest revision as of 10:47, 15 November 2023

COMPLEX OF VANCOMYCIN WITH 2-ACETOXY-D-PROPANOIC ACIDCOMPLEX OF VANCOMYCIN WITH 2-ACETOXY-D-PROPANOIC ACID

Structural highlights

1c0q is a 2 chain structure with sequence from Amycolatopsis orientalis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1Å
Ligands:, , , , , , , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

Bacterial resistance to vancomycin has been attributed to the loss of an intermolecular hydrogen bond between vancomycin and its peptidoglycan target when cell wall biosynthesis proceeds via depsipeptide intermediates rather than the usual polypeptide intermediates. To investigate the relative importance of this hydrogen bond to vancomycin binding, we have determined crystal structures at 1.0 A resolution for the vancomycin complexes with three ligands that mimic peptides and depsipeptides found in vancomycin-sensitive and vancomycin-resistant bacteria: N-acetylglycine, D-lactic acid, and 2-acetoxy-D-propanoic acid. These, in conjunction with structures that have been reported previously, indicate higher-affinity ligands elicit a structural change in the drug not seen with these low-affinity ligands. They also enable us to define a minimal set of drug-ligand interactions necessary to confer higher-affinity binding on a ligand. Most importantly, these structures point to factors in addition to the loss of an intermolecular hydrogen bond that must be invoked to explain the weaker affinity of vancomycin for depsipeptide ligands. These factors are important considerations for the design of vancomycin analogues to overcome vancomycin resistance.

Vancomycin binding to low-affinity ligands: delineating a minimum set of interactions necessary for high-affinity binding.,Loll PJ, Kaplan J, Selinsky BS, Axelsen PH J Med Chem. 1999 Nov 4;42(22):4714-9. PMID:10579833[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Loll PJ, Kaplan J, Selinsky BS, Axelsen PH. Vancomycin binding to low-affinity ligands: delineating a minimum set of interactions necessary for high-affinity binding. J Med Chem. 1999 Nov 4;42(22):4714-9. PMID:10579833

1c0q, resolution 1.00Å

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