1lmc: Difference between revisions
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New page: left|200px<br /><applet load="1lmc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lmc, resolution 2.0Å" /> '''THE CRYSTAL STRUCTURE... |
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[[Image:1lmc.gif|left|200px]]<br /><applet load="1lmc" size=" | [[Image:1lmc.gif|left|200px]]<br /><applet load="1lmc" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1lmc, resolution 2.0Å" /> | caption="1lmc, resolution 2.0Å" /> | ||
'''THE CRYSTAL STRUCTURE OF A COMPLEX BETWEEN BULGECIN, A BACTERIAL METABOLITE, AND LYSOZYME FROM THE RAINBOW TROUT'''<br /> | '''THE CRYSTAL STRUCTURE OF A COMPLEX BETWEEN BULGECIN, A BACTERIAL METABOLITE, AND LYSOZYME FROM THE RAINBOW TROUT'''<br /> | ||
==Overview== | ==Overview== | ||
Bulgecin, a sulfonated glycopeptide produced by Pseudomonas acidophila and | 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== | ==About this Structure== | ||
1LMC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oncorhynchus_mykiss Oncorhynchus mykiss] with BUL as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | 1LMC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oncorhynchus_mykiss Oncorhynchus mykiss] with <scene name='pdbligand=BUL:'>BUL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LMC OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: hydrolase (o-glycosyl)]] | [[Category: hydrolase (o-glycosyl)]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:46:16 2008'' | ||
