1lsp
From Proteopedia
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|PDB= 1lsp |SIZE=350|CAPTION= <scene name='initialview01'>1lsp</scene>, resolution 2.45Å | |PDB= 1lsp |SIZE=350|CAPTION= <scene name='initialview01'>1lsp</scene>, resolution 2.45Å | ||
|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=1lsp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lsp OCA], [http://www.ebi.ac.uk/pdbsum/1lsp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lsp RCSB]</span> | ||
}} | }} | ||
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[[Category: Karlsen, S.]] | [[Category: Karlsen, S.]] | ||
[[Category: Rao, Z H.]] | [[Category: Rao, Z H.]] | ||
| - | [[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 22:06:53 2008'' |
Revision as of 19:06, 30 March 2008
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| , resolution 2.45Å | |||||||
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| 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 BULGECIN-INHIBITED G-TYPE LYSOZYME FROM THE EGG-WHITE OF THE AUSTRALIAN BLACK SWAN. A COMPARISON OF THE BINDING OF BULGECIN TO THREE MURAMIDASES
Overview
Bulgecin A, a bacterial metabolite, has been shown to bind in the active-site groove of the chicken-type lysozyme from the rainbow trout (RBTL) and in the lysozyme-like C-terminal domain, of a soluble lytic transglycosylase (C-SLT) from Escherichia coli. These enzymes are muramidases that cleave the glycosidic bonds in the glycan strands of the murein polymer. Here we report the crystal structure of a complex between the goose-type lysozyme from the egg white of the Australian black swan (SEWL) and bulgecin A at 2.45 A resolution. As is the case for the C-SLT/bulgecin and RBTL/bulgecin complexes, the ligand binds with the N-acetylglucosamine ring in subsite C and the proline moiety in site D where it interacts with the catalytic glutamic acid. The taurine residue interacts with the beta-sheet region. Comparisons of the three buigecin complexes show that the inhibitor has the same binding mode to the muramidases with similar protein-ligand interactions, particularly for SEWL and RBTL. From our results, it seems likely that bulgecin, in general, inhibits enzymes with lysozyme-like domains and thus might represent a novel class of natural antibiotics that act on murein-degrading rather than murein-synthesizing enzymes.
About this Structure
1LSP is a Single protein structure of sequence from Cygnus atratus. Full crystallographic information is available from OCA.
Reference
Structure of a bulgecin-inhibited g-type lysozyme from the egg white of the Australian black swan. A comparison of the binding of bulgecin to three muramidases., Karlsen S, Hough E, Rao ZH, Isaacs NW, Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):105-14. PMID:15299731
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