1byl

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|ACTIVITY=
|ACTIVITY=
|GENE= SH BLE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2017 Streptoalloteichus hindustanus])
|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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|DOMAIN=
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|RELATEDENTRY=
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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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[[Category: drug sequestering]]
[[Category: drug sequestering]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:17:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:11:00 2008''

Revision as of 16:11, 30 March 2008


PDB ID 1byl

Drag the structure with the mouse to rotate
, resolution 2.3Å
Gene: SH BLE (Streptoalloteichus hindustanus)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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

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