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1t7d
From Proteopedia
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|PDB= 1t7d |SIZE=350|CAPTION= <scene name='initialview01'>1t7d</scene>, resolution 2.47Å | |PDB= 1t7d |SIZE=350|CAPTION= <scene name='initialview01'>1t7d</scene>, resolution 2.47Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ARY:ARYLOMYCIN A2'>ARY</scene> | + | |LIGAND= <scene name='pdbligand=ARY:ARYLOMYCIN+A2'>ARY</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Signal_peptidase_I Signal peptidase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.89 3.4.21.89] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Signal_peptidase_I Signal peptidase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.89 3.4.21.89] </span> |
|GENE= LEPB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= LEPB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1b12|1B12]], [[1kn9|1KN9]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t7d OCA], [http://www.ebi.ac.uk/pdbsum/1t7d PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1t7d RCSB]</span> | ||
}} | }} | ||
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[[Category: Paetzel, M.]] | [[Category: Paetzel, M.]] | ||
[[Category: Page, M G.P.]] | [[Category: Page, M G.P.]] | ||
| - | [[Category: ARY]] | ||
[[Category: antibiotic]] | [[Category: antibiotic]] | ||
[[Category: leader peptidase]] | [[Category: leader peptidase]] | ||
| Line 41: | Line 43: | ||
[[Category: signal peptide]] | [[Category: signal peptide]] | ||
| - | ''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 23:52:26 2008'' |
Revision as of 20:52, 30 March 2008
| |||||||
| , resolution 2.47Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | LEPB (Escherichia coli) | ||||||
| Activity: | Signal peptidase I, with EC number 3.4.21.89 | ||||||
| Related: | 1B12, 1KN9
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of Escherichia coli type I signal peptidase in complex with a lipopeptide inhibitor
Overview
We report here the crystallographic and biophysical analysis of a soluble, catalytically active fragment of the Escherichia coli type I signal peptidase (SPase Delta2-75) in complex with arylomycin A2. The 2.5-A resolution structure revealed that the inhibitor is positioned with its COOH-terminal carboxylate oxygen (O45) within hydrogen bonding distance of all the functional groups in the catalytic center of the enzyme (Ser90 O-gamma, Lys145 N-zeta, and Ser88 O-gamma) and that it makes beta-sheet type interactions with the beta-strands that line each side of the binding site. Ligand binding studies, calorimetry, fluorescence spectroscopy, and stopped-flow kinetics were also used to analyze the binding mode of this unique non-covalently bound inhibitor. The crystal structure was solved in the space group P4(3)2(1)2. A detailed comparison is made to the previously published acyl-enzyme inhibitor complex structure (space group: P2(1)2(1)2) and the apo-enzyme structure (space group: P4(1)2(1)2). Together this work provides insights into the binding of pre-protein substrates to signal peptidase and will prove helpful in the development of novel antibiotics.
About this Structure
1T7D is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystallographic and biophysical analysis of a bacterial signal peptidase in complex with a lipopeptide-based inhibitor., Paetzel M, Goodall JJ, Kania M, Dalbey RE, Page MG, J Biol Chem. 2004 Jul 16;279(29):30781-90. Epub 2004 May 10. PMID:15136583
Page seeded by OCA on Sun Mar 30 23:52:26 2008
Categories: Escherichia coli | Signal peptidase I | Single protein | Dalbey, R E. | Goodall, J J. | Kania, M. | Paetzel, M. | Page, M G.P. | Antibiotic | Leader peptidase | Leader peptide | Lysine general base | Non-covalently bound inhibitor | Non-ribosomal peptide synthesis | Peptide | Secondary metabolite | Ser/lys dyad | Signal peptidase | Signal peptide
