2cl2

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[[Image:2cl2.jpg|left|200px]]<br /><applet load="2cl2" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2cl2.jpg|left|200px]]
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caption="2cl2, resolution 1.35&Aring;" />
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'''ENDO-1,3(4)-BETA-GLUCANASE FROM PHANEROCHAETE CHRYSOSPORIUM, SOLVED USING NATIVE SULFUR SAD, EXHIBITING INTACT HEPTASACCHARIDE GLYCOSYLATION'''<br />
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{{Structure
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|PDB= 2cl2 |SIZE=350|CAPTION= <scene name='initialview01'>2cl2</scene>, resolution 1.35&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY= [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]
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|GENE=
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}}
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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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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2CL2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Phanerochaete_chrysosporium Phanerochaete chrysosporium]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CL2 OCA].
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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].
==Reference==
==Reference==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=17057348 17057348]
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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]
[[Category: Endo-1,3(4)-beta-glucanase]]
[[Category: Endo-1,3(4)-beta-glucanase]]
[[Category: Phanerochaete chrysosporium]]
[[Category: Phanerochaete chrysosporium]]
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[[Category: laminarin]]
[[Category: laminarin]]
[[Category: laminarinase]]
[[Category: laminarinase]]
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[[Category: pichea pastoris]]
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[[Category: pichea pastori]]
[[Category: white rot fungus]]
[[Category: white rot fungus]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:49:44 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:16:47 2008''

Revision as of 14:16, 20 March 2008

Image:2cl2.jpg


PDB ID 2cl2

Drag the structure with the mouse to rotate
, resolution 1.35Å
Activity: Endo-1,3(4)-beta-glucanase, with EC number 3.2.1.6
Coordinates: save as pdb, mmCIF, xml



ENDO-1,3(4)-BETA-GLUCANASE FROM PHANEROCHAETE CHRYSOSPORIUM, SOLVED USING NATIVE SULFUR SAD, EXHIBITING INTACT HEPTASACCHARIDE GLYCOSYLATION


Overview

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.

About this Structure

2CL2 is a Single protein structure of sequence from Phanerochaete chrysosporium. Full crystallographic information is available from OCA.

Reference

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

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