1m2x: Difference between revisions

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[[Image:1m2x.jpg|left|200px]]
{{Seed}}
[[Image:1m2x.png|left|200px]]


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{{STRUCTURE_1m2x|  PDB=1m2x  |  SCENE=  }}  
{{STRUCTURE_1m2x|  PDB=1m2x  |  SCENE=  }}  


'''Crystal Structure of the metallo-beta-lactamase BlaB of Chryseobacterium meningosepticum in complex with the inhibitor D-captopril'''
===Crystal Structure of the metallo-beta-lactamase BlaB of Chryseobacterium meningosepticum in complex with the inhibitor D-captopril===




==Overview==
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The crystal structure of the class-B beta-lactamase, BlaB, from the pathogenic bacterium, Chryseobacterium meningosepticum, in complex with the inhibitor, d-captopril, has been solved at 1.5-A resolution. The enzyme has the typical alphabeta/betaalpha metallo-beta-lactamase fold and the characteristic two metal binding sites of members of the subclass B1, in which two Zn2+ ions were identified. d-Captopril, a diastereoisomer of the commercial drug, captopril, acts as an inhibitor by displacing the catalytic hydroxyl ion required for antibiotic hydrolysis and intercalating its sulfhydryl group between the two Zn2+ ions. Interestingly, d-captopril is located on one side of the active site cleft. The x-ray structure of the complex of the closely related enzyme, IMP-1, with a mercaptocarboxylate inhibitor, which also contains a sulfhydryl group bound to the two Zn2+ ions, shows the ligand to be located on the opposite side of the active site cleft. A molecule generated by fusion of these two inhibitors would cover the entire cleft, suggesting an interesting approach to the design of highly specific inhibitors.
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{{ABSTRACT_PUBMED_12684522}}


==About this Structure==
==About this Structure==
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[[Category: Garcia-Saez, I.]]
[[Category: Garcia-Saez, I.]]
[[Category: Alpha-beta/beta-alpha fold.]]
[[Category: Alpha-beta/beta-alpha fold.]]
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