1s7f
From Proteopedia
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|PDB= 1s7f |SIZE=350|CAPTION= <scene name='initialview01'>1s7f</scene>, resolution 2.0Å | |PDB= 1s7f |SIZE=350|CAPTION= <scene name='initialview01'>1s7f</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> | + | |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= | ||
+ | |RELATEDENTRY=[[1s7k|1S7K]], [[1s7l|1S7L]], [[1s7n|1S7N]] | ||
+ | |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.]] | ||
- | [[Category: CL]] | ||
- | [[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]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''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
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, resolution 2.0Å | |||||||
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Ligands: | , | ||||||
Gene: | RimL (Salmonella typhimurium LT2) | ||||||
Related: | 1S7K, 1S7L, 1S7N
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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
Page seeded by OCA on Sun Mar 30 23:38:25 2008