1s7f
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(New page: 200px<br /><applet load="1s7f" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s7f, resolution 2.0Å" /> '''RimL- Ribosomal L7/L1...)
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Revision as of 21:53, 24 November 2007
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RimL- Ribosomal L7/L12 alpha-N-protein acetyltransferase crystal form I (apo)
Overview
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.
About this Structure
1S7F is a Single protein structure of sequence from Salmonella typhimurium lt2 with CL and MLA as ligands. Full crystallographic information is available from OCA.
Reference
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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