1t7d

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|PDB= 1t7d |SIZE=350|CAPTION= <scene name='initialview01'>1t7d</scene>, resolution 2.47&Aring;
|PDB= 1t7d |SIZE=350|CAPTION= <scene name='initialview01'>1t7d</scene>, resolution 2.47&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=ARY:ARYLOMYCIN A2'>ARY</scene>
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|LIGAND= <scene name='pdbligand=ARY:ARYLOMYCIN+A2'>ARY</scene>
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|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]
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|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=
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|RELATEDENTRY=[[1b12|1B12]], [[1kn9|1KN9]]
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|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.]]
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[[Category: ARY]]
 
[[Category: antibiotic]]
[[Category: antibiotic]]
[[Category: leader peptidase]]
[[Category: leader peptidase]]
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[[Category: signal peptide]]
[[Category: signal peptide]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:14:46 2008''
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''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

Image:1t7d.gif


PDB ID 1t7d

Drag the structure with the mouse to rotate
, 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

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