2cl2: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
m Protected "2cl2" [edit=sysop:move=sysop]
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
Line 1: Line 1:
[[Image:2cl2.png|left|200px]]
==ENDO-1,3(4)-BETA-GLUCANASE FROM PHANEROCHAETE CHRYSOSPORIUM, SOLVED USING NATIVE SULFUR SAD, EXHIBITING INTACT HEPTASACCHARIDE GLYCOSYLATION==
<StructureSection load='2cl2' size='340' side='right' caption='[[2cl2]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2cl2]] is a 1 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CL2 FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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><br>
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=2cl2 RCSB], [http://www.ebi.ac.uk/pdbsum/2cl2 PDBsum]</span></td></tr>
<table>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cl/2cl2_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


{{STRUCTURE_2cl2|  PDB=2cl2  |  SCENE=  }}
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>


===ENDO-1,3(4)-BETA-GLUCANASE FROM PHANEROCHAETE CHRYSOSPORIUM, SOLVED USING NATIVE SULFUR SAD, EXHIBITING INTACT HEPTASACCHARIDE GLYCOSYLATION===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>


{{ABSTRACT_PUBMED_17057348}}
==See Also==
 
*[[Glucanase|Glucanase]]
==About this Structure==
== References ==
[[2cl2]] is a 1 chain structure with 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].
<references/>
 
__TOC__
==Reference==
</StructureSection>
<ref group="xtra">PMID:017057348</ref><references group="xtra"/>
[[Category: Phanerochaete chrysosporium]]
[[Category: Phanerochaete chrysosporium]]
[[Category: Igarashi, K.]]
[[Category: Igarashi, K.]]

Revision as of 00:17, 30 September 2014

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

2cl2, resolution 1.35Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2cl2&oldid=2019573"