1jfx: Difference between revisions

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<StructureSection load='1jfx' size='340' side='right'caption='[[1jfx]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
<StructureSection load='1jfx' size='340' side='right'caption='[[1jfx]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1jfx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_coelicolor"_(muller_1908)_lieske_1921 "actinomyces coelicolor" (muller 1908) lieske 1921]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JFX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1JFX FirstGlance]. <br>
<table><tr><td colspan='2'>[[1jfx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JFX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JFX FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cel ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1902 "Actinomyces coelicolor" (Muller 1908) Lieske 1921])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jfx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jfx OCA], [https://pdbe.org/1jfx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jfx RCSB], [https://www.ebi.ac.uk/pdbsum/1jfx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jfx ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1jfx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jfx OCA], [http://pdbe.org/1jfx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jfx RCSB], [http://www.ebi.ac.uk/pdbsum/1jfx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jfx ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LYSM1_STRGL LYSM1_STRGL]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1jfx ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1jfx ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cellosyl is a bacterial muramidase from Streptomyces coelicolor. Similar to other lysozymes, the enzyme cleaves the beta-1,4-glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine units, but it also exhibits a beta-1,4-N,6-O-diacetylmuramidase activity. The latter enables Cellosyl to degrade the cell walls of Staphylococcus aureus, which are not hydrolyzed by chicken-, goose-, or bacteriophage T4-type lysozymes. The enzymatic activity and amino acid sequence of Cellosyl group it with lysozymes of the Chalaropsis type, for which no detailed structural information has been available so far. The crystal structure of Cellosyl from S. coelicolor has been determined to a resolution of 1.65 A and refined to an R-factor of 15.2%. The enzyme is comprised of a single domain and possesses an unusual beta/alpha-barrel fold. The last strand, beta 8, of the (beta/alpha)(5)beta(3)-barrel is found to be antiparallel to strands beta 7 and beta 1. Asp-9, Asp-98, and Glu-100 are located at the active site. The structure of Cellosyl exhibits a new lysozyme fold and represents a new class of polysaccharide-hydrolyzing beta/alpha-barrels.
A new lysozyme fold. Crystal structure of the muramidase from Streptomyces coelicolor at 1.65 A resolution.,Rau A, Hogg T, Marquardt R, Hilgenfeld R J Biol Chem. 2001 Aug 24;276(34):31994-9. Epub 2001 Jun 26. PMID:11427528<ref>PMID:11427528</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1jfx" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Lysozyme]]
[[Category: Streptomyces coelicolor]]
[[Category: Hilgenfeld, R]]
[[Category: Hilgenfeld R]]
[[Category: Hogg, T]]
[[Category: Hogg T]]
[[Category: Marquardt, R]]
[[Category: Marquardt R]]
[[Category: Rau, A]]
[[Category: Rau A]]
[[Category: Beta-alpha-barrel]]
[[Category: Cellosyl]]
[[Category: Hydrolase]]
[[Category: N-acetylmuramidase]]

Revision as of 10:51, 3 April 2024

Crystal structure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolutionCrystal structure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution

Structural highlights

1jfx is a 1 chain structure with sequence from Streptomyces coelicolor. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.65Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LYSM1_STRGL

Evolutionary Conservation

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

See Also

1jfx, resolution 1.65Å

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OCA
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