1ecs
From Proteopedia
(New page: 200px<br /><applet load="1ecs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ecs, resolution 1.70Å" /> '''THE 1.7 A CRYSTAL ST...) |
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| - | [[Image:1ecs.jpg|left|200px]]<br /><applet load="1ecs" size=" | + | [[Image:1ecs.jpg|left|200px]]<br /><applet load="1ecs" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ecs, resolution 1.70Å" /> | caption="1ecs, resolution 1.70Å" /> | ||
'''THE 1.7 A CRYSTAL STRUCTURE OF A BLEOMYCIN RESISTANCE DETERMINANT ENCODED ON THE TRANSPOSON TN5'''<br /> | '''THE 1.7 A CRYSTAL STRUCTURE OF A BLEOMYCIN RESISTANCE DETERMINANT ENCODED ON THE TRANSPOSON TN5'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The transposon Tn5 carries a gene designated ble that confers resistance | + | The transposon Tn5 carries a gene designated ble that confers resistance to bleomycin (Bm). In this study, we determined the x-ray crystal structures of the ble gene product, designated BLMT, uncomplexed and complexed with Bm at 1.7 and 2.5 A resolution, respectively. The structure of BLMT is a dimer with two Bm-binding pockets composed of two large concavities and two long grooves. This crystal structure of BLMT complexed with Bm gives a precise mode for binding of the antibiotic to BLMT. The conformational change of BLMT generated by binding to Bm occurs at a beta-turn composed of the residues from Gln(97) to Thr(102). Crystallographic analysis of Bm bound to BLMT shows that two thiazolium rings of the bithiazole moiety are in the trans conformation. The axial ligand, which binds a metal ion, seems to be the primary amine in the beta-aminoalanine moiety. This report, which is the first with regard to the x-ray crystal structure of Bm, shows that the bithiazole moiety of Bm is far from the metal-binding domain. That is, Bm complexed with BLMT takes a more extended form than the drug complexed with DNA. |
==About this Structure== | ==About this Structure== | ||
| - | 1ECS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae] with CA and PG4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1ECS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=PG4:'>PG4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ECS OCA]. |
==Reference== | ==Reference== | ||
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[[Category: arm-exchange]] | [[Category: arm-exchange]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:26:27 2008'' |
Revision as of 10:26, 21 February 2008
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THE 1.7 A CRYSTAL STRUCTURE OF A BLEOMYCIN RESISTANCE DETERMINANT ENCODED ON THE TRANSPOSON TN5
Overview
The transposon Tn5 carries a gene designated ble that confers resistance to bleomycin (Bm). In this study, we determined the x-ray crystal structures of the ble gene product, designated BLMT, uncomplexed and complexed with Bm at 1.7 and 2.5 A resolution, respectively. The structure of BLMT is a dimer with two Bm-binding pockets composed of two large concavities and two long grooves. This crystal structure of BLMT complexed with Bm gives a precise mode for binding of the antibiotic to BLMT. The conformational change of BLMT generated by binding to Bm occurs at a beta-turn composed of the residues from Gln(97) to Thr(102). Crystallographic analysis of Bm bound to BLMT shows that two thiazolium rings of the bithiazole moiety are in the trans conformation. The axial ligand, which binds a metal ion, seems to be the primary amine in the beta-aminoalanine moiety. This report, which is the first with regard to the x-ray crystal structure of Bm, shows that the bithiazole moiety of Bm is far from the metal-binding domain. That is, Bm complexed with BLMT takes a more extended form than the drug complexed with DNA.
About this Structure
1ECS is a Single protein structure of sequence from Klebsiella pneumoniae with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structures of the transposon Tn5-carried bleomycin resistance determinant uncomplexed and complexed with bleomycin., Maruyama M, Kumagai T, Matoba Y, Hayashida M, Fujii T, Hata Y, Sugiyama M, J Biol Chem. 2001 Mar 30;276(13):9992-9. Epub 2000 Dec 29. PMID:11134052
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