1ghg
From Proteopedia
(New page: 200px<br /><applet load="1ghg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ghg, resolution 0.98Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1ghg.gif|left|200px]]<br /><applet load="1ghg" size=" | + | [[Image:1ghg.gif|left|200px]]<br /><applet load="1ghg" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ghg, resolution 0.98Å" /> | caption="1ghg, resolution 0.98Å" /> | ||
'''CRYSTAL STRUCTURE OF VANCOMYCIN AGLYCON'''<br /> | '''CRYSTAL STRUCTURE OF VANCOMYCIN AGLYCON'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The sugar residues of the glycopeptide antibiotic vancomycin contribute to | + | The sugar residues of the glycopeptide antibiotic vancomycin contribute to the cooperativity of ligand binding, thereby increasing ligand affinity and enhancing antimicrobial activity. To assess the structural basis for these effects, we determined a 0.98 A X-ray crystal structure of the vancomycin aglycon and compared it to structures of several intact vancomycin:ligand complexes. The crystal structure reveals that the aglycon binds acetate anions and forms back-to-back dimeric complexes in a manner similar to that of intact vancomycin. However, the four independent copies of the aglycon in each asymmetric unit of the crystal exhibit a high degree of conformational heterogeneity. These results suggest that the sugar residues, in addition to enlarging and strengthening the dimer interface, provide steric constraints that limit the vancomycin molecule to a relatively small number of productive conformations. |
==About this Structure== | ==About this Structure== | ||
| - | 1GHG is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with VAG, DMS and ACY as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1GHG is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=VAG:'>VAG</scene>, <scene name='pdbligand=DMS:'>DMS</scene> and <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GHG OCA]. |
==Reference== | ==Reference== | ||
The role of sugar residues in molecular recognition by vancomycin., Kaplan J, Korty BD, Axelsen PH, Loll PJ, J Med Chem. 2001 May 24;44(11):1837-40. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11356118 11356118] | The role of sugar residues in molecular recognition by vancomycin., Kaplan J, Korty BD, Axelsen PH, Loll PJ, J Med Chem. 2001 May 24;44(11):1837-40. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11356118 11356118] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Axelsen, P | + | [[Category: Axelsen, P H.]] |
[[Category: Kaplan, J.]] | [[Category: Kaplan, J.]] | ||
| - | [[Category: Korty, B | + | [[Category: Korty, B D.]] |
| - | [[Category: Loll, P | + | [[Category: Loll, P J.]] |
[[Category: ACY]] | [[Category: ACY]] | ||
[[Category: DMS]] | [[Category: DMS]] | ||
| Line 22: | Line 22: | ||
[[Category: glycopeptide antibiotic]] | [[Category: glycopeptide antibiotic]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:50:07 2008'' |
Revision as of 10:50, 21 February 2008
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CRYSTAL STRUCTURE OF VANCOMYCIN AGLYCON
Overview
The sugar residues of the glycopeptide antibiotic vancomycin contribute to the cooperativity of ligand binding, thereby increasing ligand affinity and enhancing antimicrobial activity. To assess the structural basis for these effects, we determined a 0.98 A X-ray crystal structure of the vancomycin aglycon and compared it to structures of several intact vancomycin:ligand complexes. The crystal structure reveals that the aglycon binds acetate anions and forms back-to-back dimeric complexes in a manner similar to that of intact vancomycin. However, the four independent copies of the aglycon in each asymmetric unit of the crystal exhibit a high degree of conformational heterogeneity. These results suggest that the sugar residues, in addition to enlarging and strengthening the dimer interface, provide steric constraints that limit the vancomycin molecule to a relatively small number of productive conformations.
About this Structure
1GHG is a Protein complex structure of sequences from [1] with , and as ligands. Full crystallographic information is available from OCA.
Reference
The role of sugar residues in molecular recognition by vancomycin., Kaplan J, Korty BD, Axelsen PH, Loll PJ, J Med Chem. 2001 May 24;44(11):1837-40. PMID:11356118
Page seeded by OCA on Thu Feb 21 12:50:07 2008
Categories: Protein complex | Axelsen, P H. | Kaplan, J. | Korty, B D. | Loll, P J. | ACY | DMS | VAG | Aglycon | Glycopeptide antibiotic
