1s7f

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|PDB= 1s7f |SIZE=350|CAPTION= <scene name='initialview01'>1s7f</scene>, resolution 2.0&Aring;
|PDB= 1s7f |SIZE=350|CAPTION= <scene name='initialview01'>1s7f</scene>, resolution 2.0&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=MLA:MALONIC ACID'>MLA</scene>
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MLA:MALONIC+ACID'>MLA</scene>
|ACTIVITY=
|ACTIVITY=
|GENE= RimL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=99287 Salmonella typhimurium LT2])
|GENE= RimL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=99287 Salmonella typhimurium LT2])
 +
|DOMAIN=
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|RELATEDENTRY=[[1s7k|1S7K]], [[1s7l|1S7L]], [[1s7n|1S7N]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1s7f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s7f OCA], [http://www.ebi.ac.uk/pdbsum/1s7f PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1s7f RCSB]</span>
}}
}}
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[[Category: Roderick, S L.]]
[[Category: Roderick, S L.]]
[[Category: Vetting, M W.]]
[[Category: Vetting, M W.]]
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[[Category: CL]]
 
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[[Category: MLA]]
 
[[Category: acetyltransferase]]
[[Category: acetyltransferase]]
[[Category: alpha-n-protein acetyltransferase]]
[[Category: alpha-n-protein acetyltransferase]]
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[[Category: l7/l12]]
[[Category: l7/l12]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:01:28 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:38:25 2008''

Revision as of 20:38, 30 March 2008


PDB ID 1s7f

Drag the structure with the mouse to rotate
, resolution 2.0Å
Ligands: ,
Gene: RimL (Salmonella typhimurium LT2)
Related: 1S7K, 1S7L, 1S7N


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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. 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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