1k4j: Difference between revisions
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'''Crystal Structure of the Acyl-homoserinelactone Synthase EsaI Complexed with Rhenate''' | {{Structure | ||
|PDB= 1k4j |SIZE=350|CAPTION= <scene name='initialview01'>1k4j</scene>, resolution 2.5Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=REO:PERRHENATE'>REO</scene> | |||
|ACTIVITY= | |||
|GENE= esaI/esaR cluster ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=66271 Pantoea stewartii subsp. stewartii]) | |||
}} | |||
'''Crystal Structure of the Acyl-homoserinelactone Synthase EsaI Complexed with Rhenate''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1K4J is a [ | 1K4J is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pantoea_stewartii_subsp._stewartii Pantoea stewartii subsp. stewartii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K4J OCA]. | ||
==Reference== | ==Reference== | ||
Structural basis and specificity of acyl-homoserine lactone signal production in bacterial quorum sensing., Watson WT, Minogue TD, Val DL, von Bodman SB, Churchill ME, Mol Cell. 2002 Mar;9(3):685-94. PMID:[http:// | Structural basis and specificity of acyl-homoserine lactone signal production in bacterial quorum sensing., Watson WT, Minogue TD, Val DL, von Bodman SB, Churchill ME, Mol Cell. 2002 Mar;9(3):685-94. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11931774 11931774] | ||
[[Category: Pantoea stewartii subsp. stewartii]] | [[Category: Pantoea stewartii subsp. stewartii]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: quorum sensing]] | [[Category: quorum sensing]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:12:29 2008'' | ||
Revision as of 10:12, 20 March 2008
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| 1k4j, resolution 2.5Å | |||||||||||||
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| Ligands: | REO | ||||||||||||
| Gene: | esaI/esaR cluster (Pantoea stewartii subsp. stewartii) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Crystal Structure of the Acyl-homoserinelactone Synthase EsaI Complexed with Rhenate
Overview
Synthesis and detection of acyl-homoserine lactones (AHLs) enables many gram-negative bacteria to engage in quorum sensing, an intercellular signaling mechanism that activates differentiation to virulent and biofilm lifestyles. The AHL synthases catalyze acylation of S-adenosyl-L-methionine by acyl-acyl carrier protein and lactonization of the methionine moiety to give AHLs. The crystal structure of the AHL synthase, EsaI, determined at 1.8 A resolution, reveals a remarkable structural similarity to the N-acetyltransferases and defines a common phosphopantetheine binding fold as the catalytic core. Critical residues responsible for catalysis and acyl chain specificity have been identified from a modeled substrate complex and verified through functional analysis in vivo. A mechanism for the N-acylation of S-adenosyl-L-methionine by 3-oxo-hexanoyl-acyl carrier protein is proposed.
About this Structure
1K4J is a Single protein structure of sequence from Pantoea stewartii subsp. stewartii. Full crystallographic information is available from OCA.
Reference
Structural basis and specificity of acyl-homoserine lactone signal production in bacterial quorum sensing., Watson WT, Minogue TD, Val DL, von Bodman SB, Churchill ME, Mol Cell. 2002 Mar;9(3):685-94. PMID:11931774
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