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1byl
From Proteopedia
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(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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Revision as of 09:54, 20 November 2007
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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 Tue Nov 20 12:01:49 2007
