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1lmc

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Revision as of 16:13, 27 October 2021

THE CRYSTAL STRUCTURE OF A COMPLEX BETWEEN BULGECIN, A BACTERIAL METABOLITE, AND LYSOZYME FROM THE RAINBOW TROUT

Structural highlights

1lmc is a 1 chain structure with sequence from Oncorhynchus mykiss. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:	Lysozyme, with EC number 3.2.1.17
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[LYSC2_ONCMY] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has antibacterial activity against the Gram positive bacterium P.citreus. Has no antibacterial activity against the Gram negative bacteria E.coli and Y.ruckeri. Does not have hemolytic activity against trout erythrocytes.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Fernandes JM, Kemp GD, Smith VJ. Two novel muramidases from skin mucosa of rainbow trout (Oncorhynchus mykiss). Comp Biochem Physiol B Biochem Mol Biol. 2004 May;138(1):53-64. PMID:15142536 doi:http://dx.doi.org/10.1016/j.cbpc.2004.02.004
↑ Karlsen S, Hough E. Structure of a complex between bulgecin, a bacterial metabolite, and lysozyme from the rainbow trout. Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):115-23. PMID:15299732 doi:10.1107/S0907444995006366

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1lmc"

Categories: Large Structures | Lysozyme | Oncorhynchus mykiss | Hough, E | Karlsen, S

@@ Line 3: / Line 3: @@
 <StructureSection load='1lmc' size='340' side='right'caption='[[1lmc]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1lmc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oncorhynchus_mykiss Oncorhynchus mykiss]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LMC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LMC FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1lmc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oncorhynchus_mykiss Oncorhynchus mykiss]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LMC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LMC FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BUL:BULGECIN+A'>BUL</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BUL:BULGECIN+A'>BUL</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1lmc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lmc RCSB], [http://www.ebi.ac.uk/pdbsum/1lmc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1lmc ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lmc OCA], [https://pdbe.org/1lmc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lmc RCSB], [https://www.ebi.ac.uk/pdbsum/1lmc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lmc ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/LYSC2_ONCMY LYSC2_ONCMY]] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has antibacterial activity against the Gram positive bacterium P.citreus. Has no antibacterial activity against the Gram negative bacteria E.coli and Y.ruckeri. Does not have hemolytic activity against trout erythrocytes.<ref>PMID:15142536</ref>
+[[https://www.uniprot.org/uniprot/LYSC2_ONCMY LYSC2_ONCMY]] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has antibacterial activity against the Gram positive bacterium P.citreus. Has no antibacterial activity against the Gram negative bacteria E.coli and Y.ruckeri. Does not have hemolytic activity against trout erythrocytes.<ref>PMID:15142536</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1lmc

From Proteopedia

Revision as of 16:13, 27 October 2021

THE CRYSTAL STRUCTURE OF A COMPLEX BETWEEN BULGECIN, A BACTERIAL METABOLITE, AND LYSOZYME FROM THE RAINBOW TROUT

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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