4kc7 - Revision history

OCA at 12:10, 1 March 2024

OCA — Fri, 01 Mar 2024 12:10:03 GMT

←Older revision		Revision as of 12:10, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4kc7]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_petrophila_RKU-1 Thermotoga petrophila RKU-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KC7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KC7 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4kc7]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_petrophila_RKU-1 Thermotoga petrophila RKU-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KC7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KC7 FirstGlance]. <br>
-	</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=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.75Å</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=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></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=4kc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kc7 OCA], [https://pdbe.org/4kc7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kc7 RCSB], [https://www.ebi.ac.uk/pdbsum/4kc7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kc7 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=4kc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kc7 OCA], [https://pdbe.org/4kc7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kc7 RCSB], [https://www.ebi.ac.uk/pdbsum/4kc7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kc7 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/EABN_THEP1 EABN_THEP1] Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the internal cleavage of alpha-(1->5)-L-arabinofuranosyl residues in different arabinan-containing polysaccharides, and releases arabinotriose and arabinobiose as end products. It acts on branched arabinan (from sugar beet), but more slowly when compared to linear or debranched arabinan.		[https://www.uniprot.org/uniprot/EABN_THEP1 EABN_THEP1] Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the internal cleavage of alpha-(1->5)-L-arabinofuranosyl residues in different arabinan-containing polysaccharides, and releases arabinotriose and arabinobiose as end products. It acts on branched arabinan (from sugar beet), but more slowly when compared to linear or debranched arabinan.
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Arabinanases (ABNs, EC 3.2.1.99) are promising catalysts for environmental friendly biomass conversion into energy and chemicals. These enzymes catalyze the hydrolysis of the alpha-1,5-linked L-arabinofuranoside backbone of plant cell wall arabinans releasing arabino-oligosaccharides and arabinose, the second most abundant pentose in nature. In this work, new findings about the molecular mechanisms governing activation, functional differentiation and catalysis of GH43 ABNs are presented. Biophysical, mutational and biochemical studies with the hyperthermostable two-domain endo-acting ABN from Thermotoga petrophila (TpABN) revealed how some GH43 ABNs are activated by calcium ions via hyperpolarization of the catalytically-relevant histidine and the importance of the ancillary domain for catalysis and conformational stability. On the other hand, the two GH43 ABNs from rumen metagenome, ARN2 and ARN3, presented a calcium-independent mechanism in which sodium is the most likely substituent for calcium ions. The crystal structure of the two-domain endo-acting ARN2 showed that its ability to efficiently degrade branched substrates is due to a larger catalytic interface with higher accessibility than that observed in other ABNs with preference for linear arabinan. Moreover, crystallographic characterization of the single-domain exo-acting ARN3 indicated that its cleavage pattern producing arabinose is associated with the chemical recognition of reducing end of the substrate imposed by steric impediments at the aglycone-binding site. By structure-guided rational design, ARN3 was converted into a classical endo enzyme, confirming the role of the extended Arg203-Ala230 loop in determining its action mode. These results reveal novel molecular aspects concerning the functioning of GH43 ABNs and provide new strategies for arabinan degradation.
-
-	Mechanistic strategies for catalysis adopted by evolutionary distinct family 43 arabinanases.,Santos CR, Polo CC, Costa MC, Nascimento AF, Meza AN, Cota J, Hoffmam ZB, Honorato RV, Oliveira PS, Goldman GH, Gilbert HJ, Prade RA, Ruller R, Squina FM, Wong DW, Murakami MT J Biol Chem. 2014 Jan 27. PMID:24469445<ref>PMID:24469445</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4kc7" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Arabinanase 3D structures\|Arabinanase 3D structures]]		*[[Arabinanase 3D structures\|Arabinanase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 11:51, 30 November 2022

OCA — Wed, 30 Nov 2022 11:51:44 GMT

←Older revision		Revision as of 11:51, 30 November 2022
Line 1:		Line 1:

	==Crystal Structure of Endo-1,5-alpha-L-arabinanase from Thermotoga petrophila RKU-1==		==Crystal Structure of Endo-1,5-alpha-L-arabinanase from Thermotoga petrophila RKU-1==
-	<StructureSection load='4kc7' size='340' side='right' caption='[[4kc7]], [[Resolution\|resolution]] 1.75Å' scene=''>	+	<StructureSection load='4kc7' size='340' side='right'caption='[[4kc7]], [[Resolution\|resolution]] 1.75Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4kc7]] is a 3 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Thep1 Thep1~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KC7 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4KC7 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4kc7]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_petrophila_RKU-1 Thermotoga petrophila RKU-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KC7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KC7 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=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4kc8\|4kc8]], [[4kca\|4kca]], [[4kcb\|4kcb]]</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=4kc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kc7 OCA], [https://pdbe.org/4kc7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kc7 RCSB], [https://www.ebi.ac.uk/pdbsum/4kc7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kc7 ProSAT]</span></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Tpet_0637 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=390874 THEP1])</td></tr>~~	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arabinan_endo-1,5-alpha-L-arabinosidase Arabinan endo-1,5-alpha-L-arabinosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.99 3.2.1.99] </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=4kc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kc7 OCA], [~~http~~://pdbe.org/4kc7 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4kc7 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4kc7 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4kc7 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/EABN_THEP1 EABN_THEP1]] Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the internal cleavage of alpha-(1->5)-L-arabinofuranosyl residues in different arabinan-containing polysaccharides, and releases arabinotriose and arabinobiose as end products. It acts on branched arabinan (from sugar beet), but more slowly when compared to linear or debranched arabinan.	+	[https://www.uniprot.org/uniprot/EABN_THEP1 EABN_THEP1] Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the internal cleavage of alpha-(1->5)-L-arabinofuranosyl residues in different arabinan-containing polysaccharides, and releases arabinotriose and arabinobiose as end products. It acts on branched arabinan (from sugar beet), but more slowly when compared to linear or debranched arabinan.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 4kc7" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4kc7" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Arabinanase 3D structures\|Arabinanase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Arabinan endo-1,5-alpha-L-arabinosidase~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Thep1~~]]	+	[[Category: Thermotoga petrophila RKU-1]]
-	[[Category: Costa~~, M C.M F~~]]	+	[[Category: Costa MCMF]]
-	[[Category: Mesa~~, A N~~]]	+	[[Category: Mesa AN]]
-	[[Category: Murakami~~, M T~~]]	+	[[Category: Murakami MT]]
-	[[Category: Nascimento~~, A F.Z~~]]	+	[[Category: Nascimento AFZ]]
-	[[Category: Polo~~, C C~~]]	+	[[Category: Polo CC]]
-	[[Category: Prade~~, R A~~]]	+	[[Category: Prade RA]]
-	[[Category: Ruller, R]]	+	[[Category: Ruller R]]
-	[[Category: Santos~~, C R~~]]	+	[[Category: Santos CR]]
-	[[Category: Squina~~, F M]]~~	+	[[Category: Squina FM]]
-	~~[[Category: Arabinanase]]~~	+
-	~~[[Category: Beta-propeller]]~~	+
-	~~[[Category: Gh43]]~~	+
-	~~[[Category: Glycoside hydrolase]]~~	+
-	~~[[Category: Hydrolase~~]]	+

OCA at 20:06, 24 January 2018

OCA — Wed, 24 Jan 2018 20:06:23 GMT

←Older revision		Revision as of 20:06, 24 January 2018
Line 21:		Line 21:
	</div>		</div>
	<div class="pdbe-citations 4kc7" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4kc7" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Arabinanase\|Arabinanase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 22:27, 4 August 2016

OCA — Thu, 04 Aug 2016 22:27:35 GMT

←Older revision		Revision as of 22:27, 4 August 2016
Line 1:		Line 1:
		+
	==Crystal Structure of Endo-1,5-alpha-L-arabinanase from Thermotoga petrophila RKU-1==		==Crystal Structure of Endo-1,5-alpha-L-arabinanase from Thermotoga petrophila RKU-1==
	<StructureSection load='4kc7' size='340' side='right' caption='[[4kc7]], [[Resolution\|resolution]] 1.75Å' scene=''>		<StructureSection load='4kc7' size='340' side='right' caption='[[4kc7]], [[Resolution\|resolution]] 1.75Å' scene=''>
Line 7:		Line 8:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Tpet_0637 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=390874 THEP1])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Tpet_0637 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=390874 THEP1])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arabinan_endo-1,5-alpha-L-arabinosidase Arabinan endo-1,5-alpha-L-arabinosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.99 3.2.1.99] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arabinan_endo-1,5-alpha-L-arabinosidase Arabinan endo-1,5-alpha-L-arabinosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.99 3.2.1.99] </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=4kc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kc7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kc7 RCSB], [http://www.ebi.ac.uk/pdbsum/4kc7 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=4kc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kc7 OCA], [http://pdbe.org/4kc7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4kc7 RCSB], [http://www.ebi.ac.uk/pdbsum/4kc7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4kc7 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 4kc7" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Arabinanase\|Arabinanase]]		*[[Arabinanase\|Arabinanase]]
-	*[[Tubulin\|Tubulin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 20:14, 24 December 2014

OCA — Wed, 24 Dec 2014 20:14:03 GMT

←Older revision		Revision as of 20:14, 24 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4kc7\| PDB=4kc7 \| SCENE= }}~~	+	==Crystal Structure of Endo-1,5-alpha-L-arabinanase from Thermotoga petrophila RKU-1==
-	===Crystal Structure of Endo-1,5-alpha-L-arabinanase from Thermotoga petrophila RKU-1===	+	<StructureSection load='4kc7' size='340' side='right' caption='[[4kc7]], [[Resolution\|resolution]] 1.75Å' scene=''>
-	~~{{ABSTRACT_PUBMED_24469445}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4kc7]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Thep1 Thep1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KC7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KC7 FirstGlance]. <br>
-	==Function==	+	</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=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4kc8\|4kc8]], [[4kca\|4kca]], [[4kcb\|4kcb]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Tpet_0637 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=390874 THEP1])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arabinan_endo-1,5-alpha-L-arabinosidase Arabinan endo-1,5-alpha-L-arabinosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.99 3.2.1.99] </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=4kc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kc7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kc7 RCSB], [http://www.ebi.ac.uk/pdbsum/4kc7 PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
	[[http://www.uniprot.org/uniprot/EABN_THEP1 EABN_THEP1]] Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the internal cleavage of alpha-(1->5)-L-arabinofuranosyl residues in different arabinan-containing polysaccharides, and releases arabinotriose and arabinobiose as end products. It acts on branched arabinan (from sugar beet), but more slowly when compared to linear or debranched arabinan.		[[http://www.uniprot.org/uniprot/EABN_THEP1 EABN_THEP1]] Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the internal cleavage of alpha-(1->5)-L-arabinofuranosyl residues in different arabinan-containing polysaccharides, and releases arabinotriose and arabinobiose as end products. It acts on branched arabinan (from sugar beet), but more slowly when compared to linear or debranched arabinan.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Arabinanases (ABNs, EC 3.2.1.99) are promising catalysts for environmental friendly biomass conversion into energy and chemicals. These enzymes catalyze the hydrolysis of the alpha-1,5-linked L-arabinofuranoside backbone of plant cell wall arabinans releasing arabino-oligosaccharides and arabinose, the second most abundant pentose in nature. In this work, new findings about the molecular mechanisms governing activation, functional differentiation and catalysis of GH43 ABNs are presented. Biophysical, mutational and biochemical studies with the hyperthermostable two-domain endo-acting ABN from Thermotoga petrophila (TpABN) revealed how some GH43 ABNs are activated by calcium ions via hyperpolarization of the catalytically-relevant histidine and the importance of the ancillary domain for catalysis and conformational stability. On the other hand, the two GH43 ABNs from rumen metagenome, ARN2 and ARN3, presented a calcium-independent mechanism in which sodium is the most likely substituent for calcium ions. The crystal structure of the two-domain endo-acting ARN2 showed that its ability to efficiently degrade branched substrates is due to a larger catalytic interface with higher accessibility than that observed in other ABNs with preference for linear arabinan. Moreover, crystallographic characterization of the single-domain exo-acting ARN3 indicated that its cleavage pattern producing arabinose is associated with the chemical recognition of reducing end of the substrate imposed by steric impediments at the aglycone-binding site. By structure-guided rational design, ARN3 was converted into a classical endo enzyme, confirming the role of the extended Arg203-Ala230 loop in determining its action mode. These results reveal novel molecular aspects concerning the functioning of GH43 ABNs and provide new strategies for arabinan degradation.

-	~~==About this Structure==~~	+	Mechanistic strategies for catalysis adopted by evolutionary distinct family 43 arabinanases.,Santos CR, Polo CC, Costa MC, Nascimento AF, Meza AN, Cota J, Hoffmam ZB, Honorato RV, Oliveira PS, Goldman GH, Gilbert HJ, Prade RA, Ruller R, Squina FM, Wong DW, Murakami MT J Biol Chem. 2014 Jan 27. PMID:24469445<ref>PMID:24469445</ref>
-	~~[[4kc7]] is a 3 chain structure~~. ~~Full crystallographic information is available from [http~~://~~oca~~.~~weizmann~~.ac.~~il/oca-bin~~/~~ocashort?id=4KC7 OCA].~~	+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

	==See Also==		==See Also==
	*[[Arabinanase\|Arabinanase]]		*[[Arabinanase\|Arabinanase]]
-		+	*[[Tubulin\|Tubulin]]
-	==~~Reference~~==	+	== References ==
-	~~<ref group="xtra">PMID:024469445</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Arabinan endo-1,5-alpha-L-arabinosidase]]		[[Category: Arabinan endo-1,5-alpha-L-arabinosidase]]
-	[[Category: Costa, M C.M F.]]	+	[[Category: Thep1]]
-	[[Category: Mesa, A N.]]	+	[[Category: Costa, M C.M F]]
-	[[Category: Murakami, M T.]]	+	[[Category: Mesa, A N]]
-	[[Category: Nascimento, A F.Z.]]	+	[[Category: Murakami, M T]]
		+	[[Category: Nascimento, A F.Z]]
	[[Category: Polo, C C]]		[[Category: Polo, C C]]
-	[[Category: Prade, R A.]]	+	[[Category: Prade, R A]]
-	[[Category: Ruller, R.]]	+	[[Category: Ruller, R]]
-	[[Category: Santos, C R.]]	+	[[Category: Santos, C R]]
-	[[Category: Squina, F M.]]	+	[[Category: Squina, F M]]
	[[Category: Arabinanase]]		[[Category: Arabinanase]]
	[[Category: Beta-propeller]]		[[Category: Beta-propeller]]

OCA at 05:01, 9 April 2014

OCA — Wed, 09 Apr 2014 05:01:30 GMT

←Older revision		Revision as of 05:01, 9 April 2014
Line 8:		Line 8:
	==About this Structure==		==About this Structure==
	[[4kc7]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KC7 OCA].		[[4kc7]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KC7 OCA].
		+
		+	==See Also==
		+	*[[Arabinanase\|Arabinanase]]

	==Reference==		==Reference==

OCA at 11:23, 5 February 2014

OCA — Wed, 05 Feb 2014 11:23:19 GMT

←Older revision		Revision as of 11:23, 5 February 2014
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{STRUCTURE_4kc7\| PDB=4kc7 \| SCENE= }}
		+	===Crystal Structure of Endo-1,5-alpha-L-arabinanase from Thermotoga petrophila RKU-1===
		+	{{ABSTRACT_PUBMED_24469445}}

-	~~The entry 4kc7~~ is ~~ON HOLD until Paper Publication~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/EABN_THEP1 EABN_THEP1]] Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the internal cleavage of alpha-(1->5)-L-arabinofuranosyl residues in different arabinan-containing polysaccharides, and releases arabinotriose and arabinobiose as end products. It acts on branched arabinan (from sugar beet), but more slowly when compared to linear or debranched arabinan.

-	~~Authors~~: ~~Nascimento, A.F.Z., Polo, C.C, Santos, C.R., Costa, M.C.M.F., Mesa, A.N., Prade, R.A., Ruller, R., Squina, F~~.M.~~, Murakami, M~~.T.	+	==About this Structure==
		+	[[4kc7]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KC7 OCA].

-	~~Description~~: ~~Crystal Structure of Endo~~-1,5-alpha-L-~~arabinanase from Thermotoga petrophila RKU~~-1	+	==Reference==
		+	<ref group="xtra">PMID:024469445</ref><references group="xtra"/><references/>
		+	[[Category: Arabinan endo-1,5-alpha-L-arabinosidase]]
		+	[[Category: Costa, M C.M F.]]
		+	[[Category: Mesa, A N.]]
		+	[[Category: Murakami, M T.]]
		+	[[Category: Nascimento, A F.Z.]]
		+	[[Category: Polo, C C]]
		+	[[Category: Prade, R A.]]
		+	[[Category: Ruller, R.]]
		+	[[Category: Santos, C R.]]
		+	[[Category: Squina, F M.]]
		+	[[Category: Arabinanase]]
		+	[[Category: Beta-propeller]]
		+	[[Category: Gh43]]
		+	[[Category: Glycoside hydrolase]]
		+	[[Category: Hydrolase]]

OCA at 04:10, 1 August 2013

OCA — Thu, 01 Aug 2013 04:10:14 GMT

←Older revision		Revision as of 04:10, 1 August 2013
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4kc7 is ON HOLD	+	The entry 4kc7 is ON HOLD until Paper Publication

	Authors: Nascimento, A.F.Z., Polo, C.C, Santos, C.R., Costa, M.C.M.F., Mesa, A.N., Prade, R.A., Ruller, R., Squina, F.M., Murakami, M.T.		Authors: Nascimento, A.F.Z., Polo, C.C, Santos, C.R., Costa, M.C.M.F., Mesa, A.N., Prade, R.A., Ruller, R., Squina, F.M., Murakami, M.T.

	Description: Crystal Structure of Endo-1,5-alpha-L-arabinanase from Thermotoga petrophila RKU-1		Description: Crystal Structure of Endo-1,5-alpha-L-arabinanase from Thermotoga petrophila RKU-1

OCA: Protected "4kc7" [edit=sysop:move=sysop]

OCA — Thu, 02 May 2013 07:15:57 GMT

Protected "4kc7" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:15, 2 May 2013

OCA: New page: '''Unreleased structure''' The entry 4kc7 is ON HOLD Authors: Nascimento, A.F.Z., Polo, C.C, Santos, C.R., Costa, M.C.M.F., Mesa, A.N., Prade, R.A., Ruller, R., Squina, F.M., Murakami, ...

OCA — Thu, 02 May 2013 07:15:56 GMT

New page: '''Unreleased structure''' The entry 4kc7 is ON HOLD Authors: Nascimento, A.F.Z., Polo, C.C, Santos, C.R., Costa, M.C.M.F., Mesa, A.N., Prade, R.A., Ruller, R., Squina, F.M., Murakami, ...

New page

'''Unreleased structure'''

The entry 4kc7 is ON HOLD

Authors: Nascimento, A.F.Z., Polo, C.C, Santos, C.R., Costa, M.C.M.F., Mesa, A.N., Prade, R.A., Ruller, R., Squina, F.M., Murakami, M.T.

Description: Crystal Structure of Endo-1,5-alpha-L-arabinanase from Thermotoga petrophila RKU-1