1byl

<table><tr><td colspan='2'>[[1byl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"streptoalloteichus_hindustanus"_tomita_et_al._1978 "streptoalloteichus hindustanus" tomita et al. 1978]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BYL OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1BYL FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SH BLE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2017 "Streptoalloteichus hindustanus" Tomita et al. 1978])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1byl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1byl OCA], [http://pdbe.org/1byl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1byl RCSB], [http://www.ebi.ac.uk/pdbsum/1byl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1byl ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/BLE_STRHI BLE_STRHI]] Binding protein with a strong affinity to the bleomycin family of antibiotics.

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:7516875</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Streptoalloteichus hindustanus tomita et al. 1978]]

[[Category: Bergdoll, M]]

[[Category: Cagnon, C]]

[[Category: Masson, J M]]

[[Category: Antibiotic]]

[[Category: Antibiotic resistance]]

[[Category: Bleomycin]]

[[Category: Drug sequestering]]