1lmc
From Proteopedia
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|PDB= 1lmc |SIZE=350|CAPTION= <scene name='initialview01'>1lmc</scene>, resolution 2.0Å | |PDB= 1lmc |SIZE=350|CAPTION= <scene name='initialview01'>1lmc</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=BUL:BULGECIN A'>BUL</scene> | + | |LIGAND= <scene name='pdbligand=BUL:BULGECIN+A'>BUL</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lmc OCA], [http://www.ebi.ac.uk/pdbsum/1lmc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lmc RCSB]</span> | ||
}} | }} | ||
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[[Category: Hough, E.]] | [[Category: Hough, E.]] | ||
[[Category: Karlsen, S.]] | [[Category: Karlsen, S.]] | ||
| - | [[Category: BUL]] | ||
[[Category: hydrolase (o-glycosyl)]] | [[Category: hydrolase (o-glycosyl)]] | ||
| - | ''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 22:04:34 2008'' |
Revision as of 19:04, 30 March 2008
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| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Lysozyme, with EC number 3.2.1.17 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE CRYSTAL STRUCTURE OF A COMPLEX BETWEEN BULGECIN, A BACTERIAL METABOLITE, AND LYSOZYME FROM THE RAINBOW TROUT
Overview
Bulgecin, a sulfonated glycopeptide produced by Pseudomonas acidophila and Pseudomonas mesoacidophila, induces bulge formation and enhances lysis of bacterial cell walls when used in combination with beta-lactam antibiotics. The compound does not itself exhibit any antibacterial activity, but has been shown to inhibit a soluble lytic transglycosylase (SLT70) from Escherichia coli which has a lysozyme-like domain. Recently, the crystal structure of an SLT-bulgecin complex has been determined to 3.5 A resolution. We report here the crystal structure of a complex between lysozyme from the rainbow trout (RBTL) and bulgecin A at 2.0 A resolution. As for the SLT-bulgecin complex, bulgecin is bound with the glycosaminyl moiety in subsite C and the proline residue in site D of the active-site cleft of RBTL, where it makes hydrogen-bonding interactions with the catalytic residues. The taurine moiety is bound to the left side of subsites E and F in the lower part of the active-site cleft. From the observed position of the bulgecin molecule, it seems reasonable that it is an inhibitor of rainbow trout lysozyme. The lysozymes may, in general, be a target for the design of a novel type of antibiotics distinct from the beta-lactams which are insensitive to the muramidases.
About this Structure
1LMC is a Single protein structure of sequence from Oncorhynchus mykiss. Full crystallographic information is available from OCA.
Reference
Structure of a complex between bulgecin, a bacterial metabolite, and lysozyme from the rainbow trout., Karlsen S, Hough E, Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):115-23. PMID:15299732
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