1jie
From Proteopedia
(New page: 200px<br /><applet load="1jie" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jie, resolution 1.8Å" /> '''Crystal structure of ...) |
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| - | [[Image:1jie.jpg|left|200px]]<br /><applet load="1jie" size=" | + | [[Image:1jie.jpg|left|200px]]<br /><applet load="1jie" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1jie, resolution 1.8Å" /> | caption="1jie, resolution 1.8Å" /> | ||
'''Crystal structure of bleomycin-binding protein from bleomycin-producing Streptomyces verticillus complexed with metal-free bleomycin'''<br /> | '''Crystal structure of bleomycin-binding protein from bleomycin-producing Streptomyces verticillus complexed with metal-free bleomycin'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Bleomycin (Bm) in the culture broth of Streptomyces verticillus is | + | Bleomycin (Bm) in the culture broth of Streptomyces verticillus is complexed with Cu(2+) (Cu(II)). In the present study, we determined the x-ray crystal structures of the Cu(II)-bound and the metal-free types of Bm at a high resolution of 1.6 and 1.8 A, respectively, which are complexed with a Bm resistance determinant from Bm-producing S. verticillus, designated BLMA. In the current model of Cu(II).Bm complexed with BLMA, two Cu(II).Bm molecules bind to the BLMA dimer. The electron density map shows that the copper ion is clearly defined in the metal-binding domain of the Bm molecule. The metal ion is penta-coordinated by a tetragonal monopyramidal cage of nitrogens and binds to the primary amine of the beta-aminoalanine moiety of Bm. The binding experiment between Bm and BLMA showed that each of the two Bm-binding pockets has a different dissociation constant (K(d)(1) and K(d)(2)). The K(d)(1) value of 630 nm for the first Bm binding is larger than the K(d)(2) value of 120 nm, indicating that the first Bm binding gives rise to a cooperative binding of the second Bm to the other pocket. |
==About this Structure== | ==About this Structure== | ||
| - | 1JIE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_verticillus Streptomyces verticillus] with BLM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1JIE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_verticillus Streptomyces verticillus] with <scene name='pdbligand=BLM:'>BLM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JIE OCA]. |
==Reference== | ==Reference== | ||
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[[Category: protein-ligand complex]] | [[Category: protein-ligand complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:22:59 2008'' |
Revision as of 11:23, 21 February 2008
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Crystal structure of bleomycin-binding protein from bleomycin-producing Streptomyces verticillus complexed with metal-free bleomycin
Overview
Bleomycin (Bm) in the culture broth of Streptomyces verticillus is complexed with Cu(2+) (Cu(II)). In the present study, we determined the x-ray crystal structures of the Cu(II)-bound and the metal-free types of Bm at a high resolution of 1.6 and 1.8 A, respectively, which are complexed with a Bm resistance determinant from Bm-producing S. verticillus, designated BLMA. In the current model of Cu(II).Bm complexed with BLMA, two Cu(II).Bm molecules bind to the BLMA dimer. The electron density map shows that the copper ion is clearly defined in the metal-binding domain of the Bm molecule. The metal ion is penta-coordinated by a tetragonal monopyramidal cage of nitrogens and binds to the primary amine of the beta-aminoalanine moiety of Bm. The binding experiment between Bm and BLMA showed that each of the two Bm-binding pockets has a different dissociation constant (K(d)(1) and K(d)(2)). The K(d)(1) value of 630 nm for the first Bm binding is larger than the K(d)(2) value of 120 nm, indicating that the first Bm binding gives rise to a cooperative binding of the second Bm to the other pocket.
About this Structure
1JIE is a Single protein structure of sequence from Streptomyces verticillus with as ligand. Full crystallographic information is available from OCA.
Reference
The 1.6-A crystal structure of the copper(II)-bound bleomycin complexed with the bleomycin-binding protein from bleomycin-producing Streptomyces verticillus., Sugiyama M, Kumagai T, Hayashida M, Maruyama M, Matoba Y, J Biol Chem. 2002 Jan 18;277(3):2311-20. Epub 2001 Nov 12. PMID:11706014
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