2cl2

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[[Image:2cl2.jpg|left|200px]]
 
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==Endo-1,3(4)-beta-glucanase from Phanerochaete chrysosporium, solved using native sulfur SAD, exhibiting intact heptasaccharide glycosylation==
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The line below this paragraph, containing "STRUCTURE_2cl2", creates the "Structure Box" on the page.
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<StructureSection load='2cl2' size='340' side='right'caption='[[2cl2]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2cl2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Phanerodontia_chrysosporium Phanerodontia chrysosporium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CL2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CL2 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.35&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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{{STRUCTURE_2cl2| PDB=2cl2 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2cl2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cl2 OCA], [https://pdbe.org/2cl2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cl2 RCSB], [https://www.ebi.ac.uk/pdbsum/2cl2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cl2 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q874E3_PHACH Q874E3_PHACH]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cl/2cl2_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2cl2 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Laminarinase Lam16A from Phanerochaete chrysosporium was recombinantly expressed in Pichia pastoris, crystallized and the structure was solved at 1.34 A resolution using native sulfur SAD X-ray crystallography. It is the first structure of a non-specific 1,3(4)-beta-D-glucanase from glycoside hydrolase family 16 (GH16). P. chrysosporium is a wood-degrading basidiomycete fungus and Lam16A is the predominant extracellular protein expressed when laminarin is used as the sole carbon source. The protein folds into a curved beta-sandwich homologous to those of other known GH16 enzyme structures (especially kappa-carrageenase from Pseudoalteromonas carrageenovora and beta-agarase from Zobelia galactanivorans). A notable likeness is also evident with the related glycoside hydrolase family 7 (GH7) enzymes. A mammalian lectin, p58/ERGIC, as well as polysaccharide lyase (PL7) enzymes also showed significant similarity to Lam16A. The enzyme has two potential N-glycosylation sites. One such site, at Asn43, displayed a branched heptasaccharide sufficiently stabilized to be interpreted from the X-ray diffraction data. The other N-glycosylation motif was found close to the catalytic centre and is evidently not glycosylated.
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'''ENDO-1,3(4)-BETA-GLUCANASE FROM PHANEROCHAETE CHRYSOSPORIUM, SOLVED USING NATIVE SULFUR SAD, EXHIBITING INTACT HEPTASACCHARIDE GLYCOSYLATION'''
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X-ray crystallographic native sulfur SAD structure determination of laminarinase Lam16A from Phanerochaete chrysosporium.,Vasur J, Kawai R, Larsson AM, Igarashi K, Sandgren M, Samejima M, Stahlberg J Acta Crystallogr D Biol Crystallogr. 2006 Nov;62(Pt 11):1422-9. Epub 2006, Oct 18. PMID:17057348<ref>PMID:17057348</ref>
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==Overview==
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Laminarinase Lam16A from Phanerochaete chrysosporium was recombinantly expressed in Pichia pastoris, crystallized and the structure was solved at 1.34 A resolution using native sulfur SAD X-ray crystallography. It is the first structure of a non-specific 1,3(4)-beta-D-glucanase from glycoside hydrolase family 16 (GH16). P. chrysosporium is a wood-degrading basidiomycete fungus and Lam16A is the predominant extracellular protein expressed when laminarin is used as the sole carbon source. The protein folds into a curved beta-sandwich homologous to those of other known GH16 enzyme structures (especially kappa-carrageenase from Pseudoalteromonas carrageenovora and beta-agarase from Zobelia galactanivorans). A notable likeness is also evident with the related glycoside hydrolase family 7 (GH7) enzymes. A mammalian lectin, p58/ERGIC, as well as polysaccharide lyase (PL7) enzymes also showed significant similarity to Lam16A. The enzyme has two potential N-glycosylation sites. One such site, at Asn43, displayed a branched heptasaccharide sufficiently stabilized to be interpreted from the X-ray diffraction data. The other N-glycosylation motif was found close to the catalytic centre and is evidently not glycosylated.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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2CL2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Phanerochaete_chrysosporium Phanerochaete chrysosporium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CL2 OCA].
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</div>
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<div class="pdbe-citations 2cl2" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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X-ray crystallographic native sulfur SAD structure determination of laminarinase Lam16A from Phanerochaete chrysosporium., Vasur J, Kawai R, Larsson AM, Igarashi K, Sandgren M, Samejima M, Stahlberg J, Acta Crystallogr D Biol Crystallogr. 2006 Nov;62(Pt 11):1422-9. Epub 2006, Oct 18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17057348 17057348]
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*[[Glucanase 3D structures|Glucanase 3D structures]]
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[[Category: Phanerochaete chrysosporium]]
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== References ==
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[[Category: Single protein]]
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<references/>
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[[Category: Igarashi, K.]]
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__TOC__
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[[Category: Kawai, R.]]
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</StructureSection>
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[[Category: Samejima, M.]]
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[[Category: Large Structures]]
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[[Category: Sandgren, M.]]
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[[Category: Phanerodontia chrysosporium]]
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[[Category: Stahlberg, J.]]
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[[Category: Igarashi K]]
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[[Category: Vasur, J.]]
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[[Category: Kawai R]]
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[[Category: Basidiomycete]]
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[[Category: Samejima M]]
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[[Category: Beta sandwich]]
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[[Category: Sandgren M]]
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[[Category: Beta-1,3/1,6-glucan]]
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[[Category: Stahlberg J]]
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[[Category: Beta-glucanase]]
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[[Category: Vasur J]]
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[[Category: Extracellular]]
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[[Category: Family 16]]
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[[Category: Gh16]]
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[[Category: Gh7]]
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[[Category: Glycosyl hydrolase]]
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[[Category: Hydrolase]]
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[[Category: Lam16a,pichea pastori]]
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[[Category: Laminarin]]
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[[Category: Laminarinase]]
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[[Category: White rot fungus]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 22:23:47 2008''
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Current revision

Endo-1,3(4)-beta-glucanase from Phanerochaete chrysosporium, solved using native sulfur SAD, exhibiting intact heptasaccharide glycosylation

PDB ID 2cl2

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