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1byl
From Proteopedia
(New page: 200px<br /><applet load="1byl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1byl, resolution 2.3Å" /> '''BLEOMYCIN RESISTANCE ...) |
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| - | [[Image:1byl.jpg|left|200px]]<br /><applet load="1byl" size=" | + | [[Image:1byl.jpg|left|200px]]<br /><applet load="1byl" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1byl, resolution 2.3Å" /> | caption="1byl, resolution 2.3Å" /> | ||
'''BLEOMYCIN RESISTANCE PROTEIN FROM STREPTOALLOTEICHUS HINDUSTANUS'''<br /> | '''BLEOMYCIN RESISTANCE PROTEIN FROM STREPTOALLOTEICHUS HINDUSTANUS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The antibiotic bleomycin, a strong DNA cutting agent, is naturally | + | The antibiotic bleomycin, a strong DNA cutting agent, is naturally produced by actinomycetes which have developed a resistance mechanism against such a lethal compound. The crystal structure, at 2.3 A resolution, of a bleomycin resistance protein of 14 kDa reveals a structure in two halves with the same alpha/beta fold despite no sequence similarity. The crystal packing shows compact dimers with a hydrophobic interface and involved in mutual chain exchange. Two independent solution studies (analytical centrifugation and light scattering) showed that this dimeric form is not a packing artefact but is indeed the functional one. Furthermore, light scattering also showed that one dimer binds two antibiotic molecules as expected. A crevice located at the dimer interface, as well as the results of a site-directed mutagenesis study, led to a model wherein two bleomycin molecules are completely sequestered by one dimer. This provides a novel insight into antibiotic resistance due to drug sequestering, and probably also into drug transport and excretion. |
==About this Structure== | ==About this Structure== | ||
| - | 1BYL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptoalloteichus_hindustanus Streptoalloteichus hindustanus]. Full crystallographic information is available from [http:// | + | 1BYL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptoalloteichus_hindustanus Streptoalloteichus hindustanus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BYL OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Cagnon, C.]] | [[Category: Cagnon, C.]] | ||
[[Category: Dumas, P.]] | [[Category: Dumas, P.]] | ||
| - | [[Category: Masson, J | + | [[Category: Masson, J M.]] |
[[Category: antibiotic resistance]] | [[Category: antibiotic resistance]] | ||
[[Category: bleomycin]] | [[Category: bleomycin]] | ||
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[[Category: drug sequestering]] | [[Category: drug sequestering]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:00:30 2008'' |
Revision as of 10:00, 21 February 2008
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BLEOMYCIN RESISTANCE PROTEIN FROM STREPTOALLOTEICHUS HINDUSTANUS
Overview
The antibiotic bleomycin, a strong DNA cutting agent, is naturally produced by actinomycetes which have developed a resistance mechanism against such a lethal compound. The crystal structure, at 2.3 A resolution, of a bleomycin resistance protein of 14 kDa reveals a structure in two halves with the same alpha/beta fold despite no sequence similarity. The crystal packing shows compact dimers with a hydrophobic interface and involved in mutual chain exchange. Two independent solution studies (analytical centrifugation and light scattering) showed that this dimeric form is not a packing artefact but is indeed the functional one. Furthermore, light scattering also showed that one dimer binds two antibiotic molecules as expected. A crevice located at the dimer interface, as well as the results of a site-directed mutagenesis study, led to a model wherein two bleomycin molecules are completely sequestered by one dimer. This provides a novel insight into antibiotic resistance due to drug sequestering, and probably also into drug transport and excretion.
About this Structure
1BYL is a Single protein structure of sequence from Streptoalloteichus hindustanus. Full crystallographic information is available from OCA.
Reference
Crystal structure and site-directed mutagenesis of a bleomycin resistance protein and their significance for drug sequestering., Dumas P, Bergdoll M, Cagnon C, Masson JM, EMBO J. 1994 Jun 1;13(11):2483-92. PMID:7516875
Page seeded by OCA on Thu Feb 21 12:00:30 2008
