1qto

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[[Image:1qto.jpg|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qto FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qto OCA], [http://www.ebi.ac.uk/pdbsum/1qto PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qto RCSB]</span>
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'''1.5 A CRYSTAL STRUCTURE OF A BLEOMYCIN RESISTANCE DETERMINANT FROM BLEOMYCIN-PRODUCING STREPTOMYCES VERTICILLUS'''
'''1.5 A CRYSTAL STRUCTURE OF A BLEOMYCIN RESISTANCE DETERMINANT FROM BLEOMYCIN-PRODUCING STREPTOMYCES VERTICILLUS'''
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[[Category: Muta, K.]]
[[Category: Muta, K.]]
[[Category: Sugiyama, M.]]
[[Category: Sugiyama, M.]]
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[[Category: arm-exchange]]
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[[Category: Arm-exchange]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:41:31 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:18:53 2008''
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Revision as of 03:41, 3 May 2008

Template:STRUCTURE 1qto

1.5 A CRYSTAL STRUCTURE OF A BLEOMYCIN RESISTANCE DETERMINANT FROM BLEOMYCIN-PRODUCING STREPTOMYCES VERTICILLUS


Overview

Bleomycin (Bm)-binding protein, designated BLMA, which is a Bm resistance determinant from Bm-producing Streptomyces verticillus, was crystallized in a form suitable for X-ray diffraction analysis. The diffraction intensity data were collected up to a resolution of 1.5 A with a merging R-value of 0.054 at a completeness of 94 %. The BLMA structure, determined by the single isomorphous replacement method including the anomalous scattering effect (SIR-AS) at a resolution of 2.0 A, was refined at 1.5 A resolution. The final R-factor was 19.0 % and R(free) was 22.1 % including 91 water molecules. The crystal packing showed a dimer form, which was generated by arm exchange. The 1.5 A high-resolution experiment allowed an analysis of the side-chain disorder of BLMA. The structural comparison of BLMA with a homologous protein from Streptoalloteichus hindustanus, designated Shble protein, showed that a Ser100-Gly103 loop was farther from the groove, which is a Bm-binding site, in BLMA than in the Shble protein. Furthermore the hydrophobicity of the groove in BLMA is much lower than that in the Shble protein. The structural differences between these proteins may be responsible for the observation that a half-saturating concentration (K(1/2)) of Bm is higher for BLMA than for the Shble protein.

About this Structure

1QTO is a Single protein structure of sequence from Streptomyces verticillus. Full crystallographic information is available from OCA.

Reference

The 1.5 A crystal structure of a bleomycin resistance determinant from bleomycin-producing Streptomyces verticillus., Kawano Y, Kumagai T, Muta K, Matoba Y, Davies J, Sugiyama M, J Mol Biol. 2000 Jan 28;295(4):915-25. PMID:10656800 Page seeded by OCA on Sat May 3 06:41:31 2008

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