2cl2

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[[Image:2cl2.jpg|left|200px]]
 
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{{Structure
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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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|PDB= 2cl2 |SIZE=350|CAPTION= <scene name='initialview01'>2cl2</scene>, resolution 1.35&Aring;
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<StructureSection load='2cl2' size='340' side='right'caption='[[2cl2]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <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>
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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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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Endo-1,3(4)-beta-glucanase Endo-1,3(4)-beta-glucanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.6 3.2.1.6] </span>
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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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|GENE=
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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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|DOMAIN=
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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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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cl2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cl2 OCA], [http://www.ebi.ac.uk/pdbsum/2cl2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2cl2 RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/Q874E3_PHACH Q874E3_PHACH]
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== Evolutionary Conservation ==
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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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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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==Overview==
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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 ==
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.
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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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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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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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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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</div>
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[[Category: Endo-1,3(4)-beta-glucanase]]
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<div class="pdbe-citations 2cl2" style="background-color:#fffaf0;"></div>
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[[Category: Phanerochaete chrysosporium]]
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[[Category: Single protein]]
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[[Category: Igarashi, K.]]
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[[Category: Kawai, R.]]
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[[Category: Samejima, M.]]
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[[Category: Sandgren, M.]]
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[[Category: Stahlberg, J.]]
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[[Category: Vasur, J.]]
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[[Category: basidiomycete]]
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[[Category: beta sandwich]]
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[[Category: beta-1,3/1,6-glucan]]
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[[Category: beta-glucanase]]
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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 Mon Mar 31 02:22:59 2008''
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==See Also==
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*[[Glucanase 3D structures|Glucanase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Phanerodontia chrysosporium]]
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[[Category: Igarashi K]]
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[[Category: Kawai R]]
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[[Category: Samejima M]]
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[[Category: Sandgren M]]
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[[Category: Stahlberg J]]
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[[Category: Vasur J]]

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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