1n71: Difference between revisions

Revision as of 14:23, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1n71.png

Template:STRUCTURE 1n71

Crystal structure of aminoglycoside 6'-acetyltransferase type Ii in complex with coenzyme ACrystal structure of aminoglycoside 6'-acetyltransferase type Ii in complex with coenzyme A

Template:ABSTRACT PUBMED 12592013

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

OCA

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-'''Crystal structure of aminoglycoside 6'-acetyltransferase type Ii in complex with coenzyme A'''
+===Crystal structure of aminoglycoside 6'-acetyltransferase type Ii in complex with coenzyme A===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12592013}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12592013 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_12592013}}
 ==About this Structure==
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 [[Category: Antibiotic resistance]]
 [[Category: Coenzyme some]]
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