2b0q: Difference between revisions
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|PDB= 2b0q |SIZE=350|CAPTION= <scene name='initialview01'>2b0q</scene>, resolution 2.700Å | |PDB= 2b0q |SIZE=350|CAPTION= <scene name='initialview01'>2b0q</scene>, resolution 2.700Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NMY:NEOMYCIN'>NMY</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Kanamycin_kinase Kanamycin kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.95 2.7.1.95] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Kanamycin_kinase Kanamycin kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.95 2.7.1.95] </span> | ||
|GENE= aphA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1351 Enterococcus faecalis]) | |GENE= aphA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1351 Enterococcus faecalis]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1j7i|1J7I]], [[1j7l|1J7L]], [[1j7u|1J7U]], [[1l8t|1L8T]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2b0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b0q OCA], [http://www.ebi.ac.uk/pdbsum/2b0q PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2b0q RCSB]</span> | |||
}} | }} | ||
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[[Category: Berghuis, A M.]] | [[Category: Berghuis, A M.]] | ||
[[Category: Fong, D H.]] | [[Category: Fong, D H.]] | ||
[[Category: protein kinase-like]] | [[Category: protein kinase-like]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:59:52 2008'' | ||
Revision as of 01:59, 31 March 2008
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| , resolution 2.700Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | aphA (Enterococcus faecalis) | ||||||
| Activity: | Kanamycin kinase, with EC number 2.7.1.95 | ||||||
| Related: | 1J7I, 1J7L, 1J7U, 1L8T
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure Of 3',5"-Aminoglycoside Phosphotransferase Type IIIa ADP Neomycin B Complex
OverviewOverview
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.
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
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