2b0q: Difference between revisions

Revision as of 14:28, 29 July 2008

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File:2b0q.png

Template:STRUCTURE 2b0q

Crystal Structure Of 3',5"-Aminoglycoside Phosphotransferase Type IIIa ADP Neomycin B ComplexCrystal Structure Of 3',5"-Aminoglycoside Phosphotransferase Type IIIa ADP Neomycin B Complex

Template:ABSTRACT PUBMED 12006485

About this StructureAbout this Structure

2B0Q is a Single protein structure of sequence from Enterococcus faecalis. This structure supersedes the now removed PDB entry 1l8u. Full crystallographic information is available from OCA.

ReferenceReference

Substrate promiscuity of an aminoglycoside antibiotic resistance enzyme via target mimicry., Fong DH, Berghuis AM, EMBO J. 2002 May 15;21(10):2323-31. PMID:12006485

Page seeded by OCA on Tue Jul 29 14:28:36 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal Structure Of 3',5"-Aminoglycoside Phosphotransferase Type IIIa ADP Neomycin B Complex'''
+===Crystal Structure Of 3',5"-Aminoglycoside Phosphotransferase Type IIIa ADP Neomycin B Complex===
-==Overview==
+<!--
-The misuse of antibiotics has selected for bacteria that have evolved mechanisms for evading the effects of these drugs. For aminoglycosides, a group of clinically important bactericidal antibiotics that target the A-site of the 16S ribosomal RNA, the most common mode of resistance is enzyme-catalyzed chemical modification of the drug. While aminoglycosides are structurally diverse, a single enzyme can confer resistance to many of these antibiotics. For example, the aminoglycoside kinase APH(3')-IIIa, produced by pathogenic Gram-positive bacteria such as enterococci and staphylococci, is capable of detoxifying at least 10 distinct aminoglycosides. Here we describe the crystal structures of APH(3')-IIIa in complex with ADP and kanamycin A or neomycin B. These structures reveal that the basis for this enzyme's substrate promiscuity is the presence of two alternative subsites in the antibiotic binding pocket. Furthermore, comparison between the A-site of the bacterial ribosome and APH(3')-IIIa shows that mimicry is the second major factor in dictating the substrate spectrum of APH(3')-IIIa. These results suggest a potential strategy for drug design aimed at circumventing antibiotic resistance.
+The line below this paragraph, {{ABSTRACT_PUBMED_12006485}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12006485 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12006485}}
 ==About this Structure==
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 [[Category: Fong, D H.]]
 [[Category: Protein kinase-like]]
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