1ecs: Difference between revisions

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[[Image:1ecs.jpg|left|200px]]<br /><applet load="1ecs" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1ecs.jpg|left|200px]]<br /><applet load="1ecs" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1ecs, resolution 1.70Å" />

'''THE 1.7 A CRYSTAL STRUCTURE OF A BLEOMYCIN RESISTANCE DETERMINANT ENCODED ON THE TRANSPOSON TN5'''<br />

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1ECS OCA].

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==

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[[Category: arm-exchange]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 13~~:54:~~14 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:26:27 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1ecs.jpg|left|200px]]<br /><applet load="1ecs" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1ecs.jpg|left|200px]]<br /><applet load="1ecs" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1ecs, resolution 1.70&Aring;" />
 '''THE 1.7 A CRYSTAL STRUCTURE OF A BLEOMYCIN RESISTANCE DETERMINANT ENCODED ON THE TRANSPOSON TN5'''<br />
 ==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.
+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==
-ECS 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ECS OCA].
+ECS 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==
@@ Line 21: / Line 21: @@
 [[Category: arm-exchange]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:54:14 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:26:27 2008''