1byl

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[[Image:1byl.jpg|left|200px]]
[[Image:1byl.jpg|left|200px]]
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{{Structure
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|GENE= SH BLE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2017 Streptoalloteichus hindustanus])
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1byl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1byl OCA], [http://www.ebi.ac.uk/pdbsum/1byl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1byl RCSB]</span>
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'''BLEOMYCIN RESISTANCE PROTEIN FROM STREPTOALLOTEICHUS HINDUSTANUS'''
'''BLEOMYCIN RESISTANCE PROTEIN FROM STREPTOALLOTEICHUS HINDUSTANUS'''
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[[Category: Dumas, P.]]
[[Category: Dumas, P.]]
[[Category: Masson, J M.]]
[[Category: Masson, J M.]]
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[[Category: antibiotic resistance]]
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[[Category: Antibiotic resistance]]
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[[Category: bleomycin]]
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[[Category: Bleomycin]]
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[[Category: chain swapping]]
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[[Category: Chain swapping]]
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[[Category: drug sequestering]]
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[[Category: Drug sequestering]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:07:17 2008''
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Revision as of 09:07, 2 May 2008

Template:STRUCTURE 1byl

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 Fri May 2 12:07:17 2008

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