1s7n: Difference between revisions

Revision as of 21:21, 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:1s7n.png

Template:STRUCTURE 1s7n

Ribosomal L7/L12 alpha-N-protein acetyltransferase in complex with Coenzyme A (CoA free sulfhydryl)Ribosomal L7/L12 alpha-N-protein acetyltransferase in complex with Coenzyme A (CoA free sulfhydryl)

Template:ABSTRACT PUBMED 15817456

About this StructureAbout this Structure

1S7N is a Single protein structure of sequence from Salmonella typhimurium lt2. Full crystallographic information is available from OCA.

ReferenceReference

A novel dimeric structure of the RimL Nalpha-acetyltransferase from Salmonella typhimurium., Vetting MW, de Carvalho LP, Roderick SL, Blanchard JS, J Biol Chem. 2005 Jun 10;280(23):22108-14. Epub 2005 Apr 6. PMID:15817456

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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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-'''Ribosomal L7/L12 alpha-N-protein acetyltransferase in complex with Coenzyme A (CoA free sulfhydryl)'''
+===Ribosomal L7/L12 alpha-N-protein acetyltransferase in complex with Coenzyme A (CoA free sulfhydryl)===
-==Overview==
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-RimL is responsible for converting the prokaryotic ribosomal protein from L12 to L7 by acetylation of its N-terminal amino group. We demonstrate that purified RimL is capable of posttranslationally acetylating L12, exhibiting a V(max) of 21 min(-1). We have also determined the apostructure of RimL from Salmonella typhimurium and its complex with coenzyme A, revealing a homodimeric oligomer with structural similarity to other Gcn5-related N-acetyltransferase superfamily members. A large central trough located at the dimer interface provides sufficient room to bind both L12 N-terminal helices. Structural and biochemical analysis indicates that RimL proceeds by single-step transfer rather than a covalent-enzyme intermediate. This is the first structure of a Gcn5-related N-acetyltransferase family member with demonstrated activity toward a protein N(alpha)-amino group and is a first step toward understanding the molecular basis for N(alpha)acetylation and its function in cellular regulation.
+The line below this paragraph, {{ABSTRACT_PUBMED_15817456}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_15817456}}
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 [[Category: Gnat]]
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