3wmy - Revision history

OCA at 05:42, 3 August 2022

OCA — Wed, 03 Aug 2022 05:42:20 GMT

←Older revision		Revision as of 05:42, 3 August 2022
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	==Crystal Structure of Streptomyces coelicolor alpha-L-arabinofuranosidase==		==Crystal Structure of Streptomyces coelicolor alpha-L-arabinofuranosidase==
-	<StructureSection load='3wmy' size='340' side='right' caption='[[3wmy]], [[Resolution\|resolution]] 1.40Å' scene=''>	+	<StructureSection load='3wmy' size='340' side='right'caption='[[3wmy]], [[Resolution\|resolution]] 1.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3wmy]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Strco Strco]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WMY OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3WMY FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3wmy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Strco Strco]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WMY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WMY FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3wmz\|3wmz]], [[3wn0\|3wn0]], [[3wn1\|3wn1]], [[3wn2\|3wn2]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3wmz\|3wmz]], [[3wn0\|3wn0]], [[3wn1\|3wn1]], [[3wn2\|3wn2]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">abfB, SC7H1.02, SCO5932 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=100226 STRCO])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">abfB, SC7H1.02, SCO5932 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=100226 STRCO])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Non-reducing_end_alpha-L-arabinofuranosidase Non-reducing end alpha-L-arabinofuranosidase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.55 3.2.1.55] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Non-reducing_end_alpha-L-arabinofuranosidase Non-reducing end alpha-L-arabinofuranosidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.55 3.2.1.55] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3wmy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wmy OCA], [~~http~~://pdbe.org/3wmy PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3wmy RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3wmy PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3wmy ProSAT]</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=3wmy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wmy OCA], [https://pdbe.org/3wmy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wmy RCSB], [https://www.ebi.ac.uk/pdbsum/3wmy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wmy ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/EABF_STRCO EABF_STRCO]] Involved in the degradation of xylan and is a key enzyme in the complete degradation of the plant cell wall. It has a specific arabinofuranose-debranching activity on xylan from gramineae. Acts synergistically with the xylanases and binds specifically to xylan. From small arabinoxylo-oligosides (ranging from arabinoxylotriose to arabinoxylohexaose), it liberates arabinose and, after prolonged incubation, the purified enzyme exhibits some xylanolytic activity as well (By similarity).	+	[[https://www.uniprot.org/uniprot/EABF_STRCO EABF_STRCO]] Involved in the degradation of xylan and is a key enzyme in the complete degradation of the plant cell wall. It has a specific arabinofuranose-debranching activity on xylan from gramineae. Acts synergistically with the xylanases and binds specifically to xylan. From small arabinoxylo-oligosides (ranging from arabinoxylotriose to arabinoxylohexaose), it liberates arabinose and, after prolonged incubation, the purified enzyme exhibits some xylanolytic activity as well (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Non-reducing end alpha-L-arabinofuranosidase]]		[[Category: Non-reducing end alpha-L-arabinofuranosidase]]
	[[Category: Strco]]		[[Category: Strco]]

OCA at 16:46, 5 August 2016

OCA — Fri, 05 Aug 2016 16:46:54 GMT

←Older revision		Revision as of 16:46, 5 August 2016
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		+
	==Crystal Structure of Streptomyces coelicolor alpha-L-arabinofuranosidase==		==Crystal Structure of Streptomyces coelicolor alpha-L-arabinofuranosidase==
	<StructureSection load='3wmy' size='340' side='right' caption='[[3wmy]], [[Resolution\|resolution]] 1.40Å' scene=''>		<StructureSection load='3wmy' size='340' side='right' caption='[[3wmy]], [[Resolution\|resolution]] 1.40Å' scene=''>
Line 7:		Line 8:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">abfB, SC7H1.02, SCO5932 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=100226 STRCO])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">abfB, SC7H1.02, SCO5932 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=100226 STRCO])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-reducing_end_alpha-L-arabinofuranosidase Non-reducing end alpha-L-arabinofuranosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.55 3.2.1.55] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-reducing_end_alpha-L-arabinofuranosidase Non-reducing end alpha-L-arabinofuranosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.55 3.2.1.55] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wmy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wmy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wmy RCSB], [http://www.ebi.ac.uk/pdbsum/3wmy PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wmy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wmy OCA], [http://pdbe.org/3wmy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wmy RCSB], [http://www.ebi.ac.uk/pdbsum/3wmy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wmy ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 3wmy" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 04:08, 25 December 2014

OCA — Thu, 25 Dec 2014 04:08:06 GMT

←Older revision		Revision as of 04:08, 25 December 2014
Line 2:		Line 2:
	<StructureSection load='3wmy' size='340' side='right' caption='[[3wmy]], [[Resolution\|resolution]] 1.40Å' scene=''>		<StructureSection load='3wmy' size='340' side='right' caption='[[3wmy]], [[Resolution\|resolution]] 1.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3wmy]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WMY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WMY FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3wmy]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Strco Strco]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WMY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WMY FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3wmz\|3wmz]], [[3wn0\|3wn0]], [[3wn1\|3wn1]], [[3wn2\|3wn2]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3wmz\|3wmz]], [[3wn0\|3wn0]], [[3wn1\|3wn1]], [[3wn2\|3wn2]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">abfB, SC7H1.02, SCO5932 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=100226 STRCO])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-reducing_end_alpha-L-arabinofuranosidase Non-reducing end alpha-L-arabinofuranosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.55 3.2.1.55] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-reducing_end_alpha-L-arabinofuranosidase Non-reducing end alpha-L-arabinofuranosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.55 3.2.1.55] </span></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wmy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wmy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wmy RCSB], [http://www.ebi.ac.uk/pdbsum/3wmy PDBsum]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wmy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wmy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wmy RCSB], [http://www.ebi.ac.uk/pdbsum/3wmy PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/EABF_STRCO EABF_STRCO]] Involved in the degradation of xylan and is a key enzyme in the complete degradation of the plant cell wall. It has a specific arabinofuranose-debranching activity on xylan from gramineae. Acts synergistically with the xylanases and binds specifically to xylan. From small arabinoxylo-oligosides (ranging from arabinoxylotriose to arabinoxylohexaose), it liberates arabinose and, after prolonged incubation, the purified enzyme exhibits some xylanolytic activity as well (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 24:
	</StructureSection>		</StructureSection>
	[[Category: Non-reducing end alpha-L-arabinofuranosidase]]		[[Category: Non-reducing end alpha-L-arabinofuranosidase]]
-	[[Category: Fujimoto, Z.]]	+	[[Category: Strco]]
-	[[Category: Harazono, K.]]	+	[[Category: Fujimoto, Z]]
-	[[Category: Ichinose, H.]]	+	[[Category: Harazono, K]]
-	[[Category: Kaneko, S.]]	+	[[Category: Ichinose, H]]
-	[[Category: Maehara, T.]]	+	[[Category: Kaneko, S]]
-	[[Category: Michikawa, M.]]	+	[[Category: Maehara, T]]
		+	[[Category: Michikawa, M]]
	[[Category: Five-bladed beta-propeller]]		[[Category: Five-bladed beta-propeller]]
	[[Category: Glycoside hydrolase]]		[[Category: Glycoside hydrolase]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 09:25, 29 October 2014

OCA — Wed, 29 Oct 2014 09:25:05 GMT

←Older revision		Revision as of 09:25, 29 October 2014
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-	~~{{STRUCTURE_3wmy~~\| ~~PDB~~=3wmy \| ~~SCENE~~= }}	+	==Crystal Structure of Streptomyces coelicolor alpha-L-arabinofuranosidase==
-	===~~Crystal Structure of Streptomyces coelicolor~~ alpha-L-arabinofuranosidase===	+	<StructureSection load='3wmy' size='340' side='right' caption='[[3wmy]], [[Resolution\|resolution]] 1.40Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3wmy]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WMY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WMY FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3wmz\|3wmz]], [[3wn0\|3wn0]], [[3wn1\|3wn1]], [[3wn2\|3wn2]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-reducing_end_alpha-L-arabinofuranosidase Non-reducing end alpha-L-arabinofuranosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.55 3.2.1.55] </span></td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wmy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wmy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wmy RCSB], [http://www.ebi.ac.uk/pdbsum/3wmy PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	alpha-L-arabinofuranosidase, which belongs to the glycoside hydrolase family 62 (GH62), hydrolyzes arabinoxylan but not arabinan or arabinogalactan. The crystal structures of several alpha-L-arabinofuranosidases have been determined, although the structures, catalytic mechanisms, and substrate specificities of GH62 enzymes remain unclear. To evaluate the substrate specificity of a GH62 enzyme, we determined the crystal structure of alpha-L-arabinofuranosidase, which comprises a carbohydrate-binding module family 13 domain at its N terminus and a catalytic domain at its C terminus, from Streptomyces coelicolor. The catalytic domain was a five-bladed beta-propeller consisting of five radially oriented anti-parallel beta-sheets. Sugar complex structures with l-arabinose, xylotriose, and xylohexaose revealed five subsites in the catalytic cleft and an l-arabinose-binding pocket at the bottom of the cleft. The entire structure of this GH62 family enzyme was very similar to that of glycoside hydrolase 43 family enzymes, and the catalytically important acidic residues found in family 43 enzymes were conserved in GH62. Mutagenesis studies revealed that Asp(202) and Glu(361) were catalytic residues, and Trp(270), Tyr(461), and Asn(462) were involved in the substrate-binding site for discriminating the substrate structures. In particular, hydrogen bonding between Asn(462) and xylose at the nonreducing end subsite +2 was important for the higher activity of substituted arabinofuranosyl residues than that for terminal arabinofuranoses.

-	~~==Function==~~	+	Crystal structure and characterization of the glycoside hydrolase family 62 alpha-L-arabinofuranosidase from Streptomyces coelicolor.,Maehara T, Fujimoto Z, Ichinose H, Michikawa M, Harazono K, Kaneko S J Biol Chem. 2014 Mar 14;289(11):7962-72. doi: 10.1074/jbc.M113.540542. Epub 2014, Jan 30. PMID:24482228<ref>PMID:24482228</ref>
-	~~[[http://www.uniprot.org/uniprot/EABF_STRCO EABF_STRCO]] Involved in the degradation of xylan~~ and ~~is a key enzyme in the complete degradation~~ of the ~~plant cell wall. It has a specific arabinofuranose~~-~~debranching activity on xylan~~ from ~~gramineae~~. ~~Acts synergistically with the xylanases and binds specifically to xylan. From small arabinoxylo-oligosides (ranging from arabinoxylotriose to arabinoxylohexaose)~~, ~~it liberates arabinose and~~, ~~after prolonged incubation~~, ~~the purified enzyme exhibits some xylanolytic activity as well~~ (~~By similarity~~).	+

-	==~~About this Structure~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[3wmy]] is a 1 chain structure. Full crystallographic information is available from [http:~~//~~oca.weizmann.ac.il/oca-bin/ocashort?id=3WMY OCA].~~	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Non-reducing end alpha-L-arabinofuranosidase]]		[[Category: Non-reducing end alpha-L-arabinofuranosidase]]
	[[Category: Fujimoto, Z.]]		[[Category: Fujimoto, Z.]]

OCA at 11:27, 5 February 2014

OCA — Wed, 05 Feb 2014 11:27:50 GMT

←Older revision		Revision as of 11:27, 5 February 2014
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-	~~'''Unreleased structure'''~~	+	{{STRUCTURE_3wmy\| PDB=3wmy \| SCENE= }}
		+	===Crystal Structure of Streptomyces coelicolor alpha-L-arabinofuranosidase===

-	~~The entry 3wmy~~ is ~~ON HOLD until Paper Publication~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/EABF_STRCO EABF_STRCO]] Involved in the degradation of xylan and is a key enzyme in the complete degradation of the plant cell wall. It has a specific arabinofuranose-debranching activity on xylan from gramineae. Acts synergistically with the xylanases and binds specifically to xylan. From small arabinoxylo-oligosides (ranging from arabinoxylotriose to arabinoxylohexaose), it liberates arabinose and, after prolonged incubation, the purified enzyme exhibits some xylanolytic activity as well (By similarity).

-	~~Authors~~: Fujimoto, Z., ~~Maehara, T~~., Ichinose, H., ~~Michikawa, M~~., ~~Harazono, K~~., ~~Kaneko, S~~.	+	==About this Structure==
-		+	[[3wmy]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WMY OCA].
-	~~Description~~: ~~Crystal Structure of Streptomyces coelicolor alpha~~-L-~~arabinofuranosidase~~	+	[[Category: Non-reducing end alpha-L-arabinofuranosidase]]
		+	[[Category: Fujimoto, Z.]]
		+	[[Category: Harazono, K.]]
		+	[[Category: Ichinose, H.]]
		+	[[Category: Kaneko, S.]]
		+	[[Category: Maehara, T.]]
		+	[[Category: Michikawa, M.]]
		+	[[Category: Five-bladed beta-propeller]]
		+	[[Category: Glycoside hydrolase]]
		+	[[Category: Hydrolase]]

OCA at 07:22, 15 January 2014

OCA — Wed, 15 Jan 2014 07:22:32 GMT

←Older revision		Revision as of 07:22, 15 January 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3wmy is ON HOLD	+	The entry 3wmy is ON HOLD until Paper Publication

	Authors: Fujimoto, Z., Maehara, T., Ichinose, H., Michikawa, M., Harazono, K., Kaneko, S.		Authors: Fujimoto, Z., Maehara, T., Ichinose, H., Michikawa, M., Harazono, K., Kaneko, S.

	Description: Crystal Structure of Streptomyces coelicolor alpha-L-arabinofuranosidase		Description: Crystal Structure of Streptomyces coelicolor alpha-L-arabinofuranosidase

OCA: Protected "3wmy" [edit=sysop:move=sysop]

OCA — Wed, 11 Dec 2013 12:44:05 GMT

Protected "3wmy" [edit=sysop:move=sysop]

←Older revision

Revision as of 12:44, 11 December 2013

OCA: New page: '''Unreleased structure''' The entry 3wmy is ON HOLD Authors: Fujimoto, Z., Maehara, T., Ichinose, H., Michikawa, M., Harazono, K., Kaneko, S. Description: Crystal Structure of Strepto...

OCA — Wed, 11 Dec 2013 12:44:03 GMT

New page: '''Unreleased structure''' The entry 3wmy is ON HOLD Authors: Fujimoto, Z., Maehara, T., Ichinose, H., Michikawa, M., Harazono, K., Kaneko, S. Description: Crystal Structure of Strepto...

New page

'''Unreleased structure'''

The entry 3wmy is ON HOLD

Authors: Fujimoto, Z., Maehara, T., Ichinose, H., Michikawa, M., Harazono, K., Kaneko, S.

Description: Crystal Structure of Streptomyces coelicolor alpha-L-arabinofuranosidase