1n71: Difference between revisions
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'''Crystal structure of aminoglycoside 6'-acetyltransferase type Ii in complex with coenzyme A''' | {{Structure | ||
|PDB= 1n71 |SIZE=350|CAPTION= <scene name='initialview01'>1n71</scene>, resolution 1.80Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=COA:COENZYME A'>COA</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Crystal structure of aminoglycoside 6'-acetyltransferase type Ii in complex with coenzyme A''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1N71 is a [ | 1N71 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecium Enterococcus faecium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N71 OCA]. | ||
==Reference== | ==Reference== | ||
X-ray structure of the AAC(6')-Ii antibiotic resistance enzyme at 1.8 A resolution; examination of oligomeric arrangements in GNAT superfamily members., Burk DL, Ghuman N, Wybenga-Groot LE, Berghuis AM, Protein Sci. 2003 Mar;12(3):426-37. PMID:[http:// | X-ray structure of the AAC(6')-Ii antibiotic resistance enzyme at 1.8 A resolution; examination of oligomeric arrangements in GNAT superfamily members., Burk DL, Ghuman N, Wybenga-Groot LE, Berghuis AM, Protein Sci. 2003 Mar;12(3):426-37. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12592013 12592013] | ||
[[Category: Enterococcus faecium]] | [[Category: Enterococcus faecium]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: aminoglycoside 6'-n-acetyltransferase]] | [[Category: aminoglycoside 6'-n-acetyltransferase]] | ||
[[Category: antibiotic resistance]] | [[Category: antibiotic resistance]] | ||
[[Category: coenzyme | [[Category: coenzyme some]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:52:57 2008'' | ||
Revision as of 13:53, 20 March 2008
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of aminoglycoside 6'-acetyltransferase type Ii in complex with coenzyme A
OverviewOverview
The rise of antibiotic resistance as a public health concern has led to increased interest in studying the ways in which bacteria avoid the effects of antibiotics. Enzymatic inactivation by several families of enzymes has been observed to be the predominant mechanism of resistance to aminoglycoside antibiotics such as kanamycin and gentamicin. Despite the importance of acetyltransferases in bacterial resistance to aminoglycoside antibiotics, relatively little is known about their structure and mechanism. Here we report the three-dimensional atomic structure of the aminoglycoside acetyltransferase AAC(6')-Ii in complex with coenzyme A (CoA). This structure unambiguously identifies the physiologically relevant AAC(6')-Ii dimer species, and reveals that the enzyme structure is similar in the AcCoA and CoA bound forms. AAC(6')-Ii is a member of the GCN5-related N-acetyltransferase (GNAT) superfamily of acetyltransferases, a diverse group of enzymes that possess a conserved structural motif, despite low sequence homology. AAC(6')-Ii is also a member of a subset of enzymes in the GNAT superfamily that form multimeric complexes. The dimer arrangements within the multimeric GNAT superfamily members are compared, revealing that AAC(6')-Ii forms a dimer assembly that is different from that observed in the other multimeric GNAT superfamily members. This different assembly may provide insight into the evolutionary processes governing dimer formation.
About this StructureAbout this Structure
1N71 is a Single protein structure of sequence from Enterococcus faecium. Full crystallographic information is available from OCA.
ReferenceReference
X-ray structure of the AAC(6')-Ii antibiotic resistance enzyme at 1.8 A resolution; examination of oligomeric arrangements in GNAT superfamily members., Burk DL, Ghuman N, Wybenga-Groot LE, Berghuis AM, Protein Sci. 2003 Mar;12(3):426-37. PMID:12592013
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